Multiple Choice Questions in Biochemistry RC Gupta
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_FM1Multiple Choice Questions in BIOCHEMISTRY
_FM2Multiple Choice Questions in BIOCHEMISTRY
Second Edition
RC Gupta MD Professor and Head Department of Biochemistry Govt. Medical College Kota (Rajasthan)
_FM3Published by
Jitendar P Vij
Jaypee Brothers Medical Publishers (P) Ltd
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Multiple Choice Questions in Biochemistry
© 2004, RC Gupta
All rights reserved. No part of this publication should be reproduced, stored in a retrieval system, or transmitted in any form or by any means: electronic, mechanical, photocopying, recording, or otherwise, without the prior written permission of the author and the publisher.
This book has been published in good faith and belief that the material provided by author is original. Every effort is made to ensure accuracy of material, but the publisher, printer and author will not be held responsible for any inadvertent error(s). In case of any dispute, all legal matters to be settled under Delhi jurisdiction only.
First Edition: 2000
Second Edition: 2004
9788180613357
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_FM4Foreword
It gives me immense pleasure to write a Foreword to Multiple Choice Questions in Biochemistry written by Prof RC Gupta of Govt, Medical College, Kota.
Medical students have traditionally depended upon Western books for knowledge and information. The situation is changing now as a number of Indian authors have written excellent books on various branches of medical science including Biochemistry in recent years. However, an area that hasn't received adequate attention is Multiple Choice Questions. With the emphasis shifting to objective methods of assessment, there is a need for quality books on MCQs. Dr Gupta has filled a vital gap by writing this book.
I am glad to note that the coverage of the subject in this book is exhaustive and balanced. While topics like vitamins, minerals, diet and nutrition, still important in developing countries, find adequate coverage, rapidly advancing areas like recombinant DNA technology, immunochemistry and cancer have not been ignored. Referenced answers add to the value of the book.
I am sure that the book will fully meet the requirement of students preparing for 1st year MBBS and Pre-PG Entrance Examinations.
MR Soangra
Principal and Controller
Govt. Medical College and Associated Group of Hospitals
Kota (Rajasthan)
_FM5Preface to the First Edition
Multiple choice questions (MCQs) constitute an important method for objective assessment of an examinee's knowledge. Looking to the pitfalls of traditional question papers comprising of a small number of long questions, educationists are laying stress on MCQs to broaden the coverage of syllabi, to test the analytical thinking of examinees and to reduce the element of subjectivity in the system of assessment. Medical Council of India, in its Regulations on Graduate Medical Education, 1997, has also recommended the inclusion of objective type of questions in examinations. Many universities have started including MCQs in undergraduate medical examinations, and others are likely to follow suit. Moreover, entrance examinations for postgraduate medical courses are generally based on MCQs alone.
Considering the importance of MCQs in examinations, the present book has been written to provide a comprehensive question bank to students covering nearly the entire syllabus in Biochemistry with the hope that the book will help the students in preparing themselves for objective type of questions, in assessing their level of preparedness for examinations and in quick revision of the subject.
I have received help and encouragement from many quarters in writing this book. Dr MR Soangra, Principal and Controller, Govt. Medical College and Associated Group of Hospitals, Kota has been a source of inspiration and encouragement to me. I am grateful to him for his help and for his kind gesture of writing the Foreword.
I have had the benefit of wise counsel, scholarly criticism and constructive suggestions from many friends and professional colleagues. I owe a debt of gratitude to Dr NC Shah (Surat), Dr BL Sharma (Rajkot), Dr GP Singh (Rohtak), Dr Harbans Lal (Rohtak), Dr CR Vyas (Bikaner), Dr SC Vij (Bikaner), Dr VD Bohra (Jaipur), Dr VS Chowdhary (Ajmer), and Dr KL Mali (Udaipur) for reviewing various chapters of the book. However, for the errors still present, the responsibility is mine._FM6
I am thankful to Dr AS Rathore and Dr Usha Gupta for their help in proofreading. Mr Akhil Sharma, Mr Vijay Matai and Mr Anil Garg deserve appreciation and thanks for their efficient secretarial assistance. I am thankful to M/s Jaypee Brothers Medical Publishers (P) Ltd for the efforts they have made to bring the book to its present shape.
I heartily welcome comments, criticism and suggestions from the readers.
RC Gupta
_FM7Preface to the Second Edition
It gives me immense pleasure to put the second edition of Multiple Choice Questions in Biochemistry in the hands of readers. I am gratified by the response of the readers to the first edition. I am particularly thankful to the colleagues and friends who have pointed out deficiencies and have suggested improvements. I have tried my best to make this edition errorfree. A number of questions have been replaced or substantially revised. About 300 new questions have been added. A new chapter on metabolism of xenobiotics has also been added. As before, I will welcome criticism, comments and suggestions.
RC Gupta

Chemistry of Carbohydrates1

  1. Number of asymmetric carbon atoms in glucose is:
    1. One
    2. Two
    3. Three
    4. Four
(Ref. 1, p. 150)
  1. β-1, 4-Glycosidic bond is present in:
    1. Maltose
    2. Lactose
    3. Sucrose
    4. None of the above
(Ref. 1, p. 155)
  1. Number of stereoisomers of glucose is:
    1. 4
    2. 8
    3. 16
    4. None of the above
(Ref. 1, p. 150)
  1. A homopolysaccharide made up of fructose is:
    1. Glycogen
    2. Dextrin
    3. Cellulose
    4. Inulin
(Ref. 1, p. 155)
  1. Aglycone portion in methyl glucoside is:
    1. Glucose
    2. Methanol
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 153)
  1. Identical osazones are formed by:
    1. Glucose and fructose
    2. Glucose and mannose
    3. Mannose and fructose
    4. All of the above
(Ref. 4, p. 99)
1 D
2 B
3 C
4 D
5 B
6 D
2
  1. Maltose can be formed by hydrolysis of:
    1. Starch
    2. Dextrin
    3. Glycogen
    4. All of the above
(Ref. 3, p. 288)
  1. α-1, 6-Glycosidic bond is not present in:
    1. Glycogen
    2. Dextrin
    3. Amylose
    4. Amylopectin
(Ref. 1, pp. 155-156)
  1. Sulphated iduronic acid is present in:
    1. Hyaluronic acid
    2. Chondroitin sulphate
    3. Heparin
    4. All of the above
(Ref. 1, p. 158)
  1. Monosaccharides can be separated by:
    1. Electrophoresis
    2. Chromatography
    3. Salting out
    4. None of the above
(Ref. 4, p. 106)
  1. Fructose is present in hydrolysate of:
    1. Sucrose
    2. Inulin
    3. Both of the above
    4. Neither of the above
(Ref. 1, pp. 155-156)
  1. N-Acetylgalactosamine sulphate is present in:
    1. Hyaluronic acid
    2. Heparin
    3. Chondroitin sulphate
    4. None of the above
(Ref. 1, p. 158)
  1. Invertase catalyses the hydrolysis of:
    1. Maltose
    2. Lactose
    3. Sucrose
    4. None of the above
(Ref. 3, p. 299)
  1. In fructofuranose, anomeric carbon atom is:
    1. Carbon 1
    2. Carbon 2
    3. Carbon 3
    4. Carbon 4
(Ref. 1, p. 151)
  1. A carbohydrate found in DNA is:
    1. Ribose
    2. Deoxyribose
    3. Ribulose
    4. All of the above
(Ref. 1, p. 154)
7 D
8 C
9 C
10 B
11 C
12 C
13 C
14 B
15 B
3
  1. A monosaccharide not having D- and L-isomers is:
    1. Ribose
    2. Deoxyribose
    3. Erythrose
    4. Dihydroxyacetone
(Ref. 3, pp. 279-280)
  1. Ribulose is a:
    1. Ketotetrose
    2. Aldotetrose
    3. Ketopentose
    4. Aldopentose
(Ref. 1, p. 149)
  1. In D-glyceraldehyde, –OH group is present on the right hand side of carbon atom number:
    1. 1
    2. 2
    3. 3
    4. 1, 2 and 3
(Ref. 1, p. 150)
  1. A disaccharide made up of two glucose units is:
    1. Sucrose
    2. Maltose
    3. Lactose
    4. Dextrin
(Ref. 1, p. 155)
  1. A carbohydrate, commonly known as dextrose, is:
    1. Dextrin
    2. D-Fructose
    3. D-Glucose
    4. Glycogen
(Ref. 1, p. 151)
  1. Amino sugars are present in:
    1. Hyaluronic acid
    2. Chondroitin sulphate
    3. Erythromycin
    4. All of the above
(Ref. 1, p. 154)
  1. A carbohydrate found only in milk is:
    1. Glucose
    2. Galactose
    3. Lactose
    4. Maltose
(Ref. 3, p. 284)
  1. A carbohydrate, known commonly as invert sugar, is:
    1. Fructose
    2. Sucrose
    3. Glucose
    4. Lactose
(Ref. 1, p. 154)
  1. A homopolysaccharide among the following is:
    1. Heparin
    2. Hyaluronic acid
    3. Dermatan sulphate
    4. Cellulose
(Ref. 3, pp. 291, 296-297)
16 D
17 C
18 B
19 B
20 C
21 D
22 C
23 B
24 D
4
  1. A heteropolysaccharide among the following is:
    1. Inulin
    2. Cellulose
    3. Heparin
    4. Dextrin
(Ref. 4, p. 102)
  1. The predominant form of glucose in solution is:
    1. Acyclic form
    2. Hydrated acyclic form
    3. Glucofuranose
    4. Glucopyranose
(Ref. 1, p. 151)
  1. Optical isomerism is denoted by:
    1. D- and L-
    2. d- and 1-
    3. (+) and (-)
    4. Any of the above
(Ref. 1, p. 150)
  1. An L-isomer of monosaccharide formed in human body is:
    1. L-Fructose
    2. L-Erythrose
    3. L-Xylose
    4. L-Xylulose
(Ref. 1, p. 153)
  1. A pentose found in nucleotides is:
    1. D-Ribose
    2. L-Ribose
    3. D-Ribulose
    4. L-Ribulose
(Ref. 1, p. 153)
  1. The following causes laevorotation:
    1. D-Fructose
    2. L-Glucose
    3. L-Ribose
    4. All of the above
(Ref. 1, p. 150)
  1. In straight chain structure of D-glucose, –OH group is present on left hand side of carbon atom number:
    1. 2
    2. 3
    3. 4
    4. 5
(Ref. 1, p. 150)
  1. In straight chain structure of D-ribose, –OH group is present on right hand side of carbon atom number:
    1. 2
    2. 3
    3. 4
    4. All of the above
(Ref. 3, p. 280)
25 C
26 C
27 C
28 D
29 A
30 D
31 B
32 D
5
  1. The carbon atom which becomes asymmetric when the straight chain form of monosaccharide changes into ring form is known as:
    1. Anomeric carbon atom
    2. Epimeric carbon atom
    3. Isomeric carbon atom
    4. None of the above
(Ref. 1, p. 151)
  1. In α-D-glucopyranose, –OH groups projecting below the plane of the ring, are attached to carbon atoms:
    1. 1, 2 and 3
    2. 1, 2 and 4
    3. 2, 3 and 4
    4. 1, 2 and 5
(Ref. 1, p. 151)
  1. In glucopyranose, the anomeric carbon is:
    1. Carbon 1
    2. Carbon 2
    3. Carbon 5
    4. Carbon 6
(Ref. 1, p. 151)
  1. The smallest monosaccharide having furanose ring structure is:
    1. Erythrose
    2. Ribose
    3. Glucose
    4. Fructose
(Ref. 2, pp. 466-468)
  1. The specific rotation of α-D-glucopyranose is:
    1. +19
    2. +52.5
    3. +92
    4. +112
(Ref. 3, p. 282)
  1. The specific rotation of β-D-glucopyranose is:
    1. +19
    2. +52.5
    3. +92
    4. +112
(Ref. 3, p. 282)
  1. The ratio of α-D-glucopyranose to β-D-glucopyranose at equilibrium is nearly:
    1. 2:1
    2. 1:1
    3. 1:2
    4. 1:1.5
(Ref. 3, p. 282)
  1. The following is an epimeric pair:
    1. Glucose and fructose
    2. Glucose and galactose
    3. Galactose and mannose
    4. Lactose and maltose
(Ref. 1, p. 151)
33 A
34 B
35 A
36 B
37 D
38 A
39 C
40 B
6
  1. Similar osazones are formed by:
    1. Glucose and mannose
    2. Mannose and galactose
    3. Glucose and galactose
    4. None of the above
(Ref. 4, p. 99)
  1. α-Glycosidic bond is present in:
    1. Lactose
    2. Maltose
    3. Sucrose
    4. All of the above
(Ref. 1, p. 155)
  1. Branching occurs in glycogen approximately after every:
    1. Five glucose units
    2. Ten glucose units
    3. Fifteen glucose units
    4. Twenty glucose units
(Ref. 2, p. 472)
  1. Mucopolysaccharides are also known as:
    1. Mucoproteins
    2. Glycoproteins
    3. Glycosaminoglycans
    4. Homopolysaccharides
(Ref. 1, p. 156)
  1. N-Acetylglucosamine is present in:
    1. Hyaluronic acid
    2. Chondroitin sulphate
    3. Heparin
    4. All of the above
(Ref. 1, p. 158)
  1. α-Iduronic acid is present in:
    1. Hyaluronic acid
    2. Chondroitin sulphate
    3. Dermatan sulphate
    4. Keratan sulphate
(Ref. 1, pp. 703-704)
  1. Iodine gives a red colour with:
    1. Starch
    2. Dextrin
    3. Glycogen
    4. Inulin
(Ref. 4, p. 102)
41 A
42 B
43 B
44 C
45 A
46 C
47 C
7
  1. Amylose is a constituent of:
    1. Starch
    2. Cellulose
    3. Glycogen
    4. None of the above
(Ref. 1, p. 155)
  1. A homopolymer of glucose is:
    1. Starch
    2. Dextrin
    3. Glycogen
    4. All of the above
(Ref. 1, p. 155)
  1. Synovial fluid contains:
    1. Heparin
    2. Hyaluronic acid
    3. Chondroitin sulphate
    4. Keratan sulphate
(Ref. 1, pp. 703-704)
48 A
49 D
50 B

Chemistry of Lipids2

  1. The following is a polyunsaturated fatty acid:
    1. Palmitic acid
    2. Palmitoleic acid
    3. Linoleic acid
    4. Oleic acid
(Ref. 1, p. 162)
  1. The following is not a polyunsaturated fatty acid:
    1. Linoleic acid
    2. Palmitoleic acid
    3. Linolenic acid
    4. Arachidonic acid
(Ref. 1, p. 162)
  1. The following is omega-3 polyunsaturated fatty acid:
    1. Linoleic acid
    2. α-Linolenic acid
    3. γ-Linolenic acid
    4. Arachidonic acid
(Ref. 1, p. 162)
  1. A good source of polyunsaturated fatty acids is:
    1. Butter
    2. Coconut oil
    3. Cottonseed oil
    4. Hydrogenated vegetable oils
(Ref. 1, p. 162)
  1. Triglycerides are:
    1. Heavier than water
    2. Major constituents of membranes
    3. Non-polar
    4. Hydrophilic
(Ref. 3, pp. 306-307)
  1. The following is a glycerophospholipid:
    1. Lecithin
    2. Phosphatidyl inositol
    3. Cardiolipin
    4. All of the above
(Ref. 1, pp. 164-165)
1 C
2 B
3 B
4 C
5 C
6 D
9
  1. Cerebronic acid is present in:
    1. Glycerophospholipids
    2. Sphingophospholipids
    3. Galactosyl ceramide
    4. Gangliosides
(Ref. 1, p. 166)
  1. N-Acetylneuraminic acid is present in:
    1. Phospholipids
    2. Cerebrosides
    3. Gangliosides
    4. Triglycerides
(Ref. 1, p. 166)
  1. Sphingosine is not present in:
    1. Cephalin
    2. Sphingomyelin
    3. Cerebrosides
    4. Sulphatides
(Ref. 1, pp. 164-166)
  1. Acylsphingosine is also known as:
    1. Sphingomyelin
    2. Ceramide
    3. Cerebroside
    4. Sulphatide
(Ref. 1, p. 167)
  1. Specific gravity of very low density lipoproteins is:
    1. 0.95-1.006
    2. 1.006-1.063
    3. Below 0.95
    4. Above 1.063
(Ref. 1, p. 269)
  1. Protein content of low density lipoproteins is about:
    1. 1%
    2. 7-10%
    3. 21%
    4. 33-57%
(Ref. 1, p. 269)
  1. Lipid content of chylomicrons is about:
    1. 45%
    2. 75%
    3. 90%
    4. 99%
(Ref. 1, p. 269)
  1. The highest phospholipid content is found in:
    1. Chylomicrons
    2. VLDL
    3. LDL
    4. HDL
(Ref. 1, p. 269)
  1. The major lipid in chylomicrons is:
    1. Triglycerides
    2. Phospholipids
    3. Cholesterol
    4. Free fatty acids
(Ref. 1, p. 269)
7C
8C
9A
10 B
11 A
12 C
13 D
14 D
15A
10
  1. Pre-β-lipoproteins are the same as:
    1. Chylomicrons
    2. Very low density lipoproteins
    3. Low density lipoproteins
    4. High density lipoproteins
(Ref. 1, p. 268)
  1. Number of carbon atoms in cholesterol is:
    1. 17
    2. 19
    3. 27
    4. 30
(Ref. 1, p. 288)
  1. The lipoprotein richest in cholesterol is:
    1. Chylomicrons
    2. VLDL
    3. LDL
    4. HDL
(Ref. 1, p. 269)
  1. Free fatty acids are transported in circulation by:
    1. Albumin
    2. HDL
    3. LDL
    4. VLDL
(Ref. 1, p. 271)
  1. The major storage form of lipids is:
    1. Esterified cholesterol
    2. Glycerophospholipids
    3. Triglycerides
    4. Sphingolipids
(Ref. 1, p. 170)
  1. Cerebronic acid is present in:
    1. Triglycerides
    2. Galactosylceramide
    3. Esterified cholesterol
    4. Sphingomyelin
(Ref. 1, p. 166)
  1. Sphingosine is present in:
    1. Lecithin
    2. Cephalin
    3. Ceramide
    4. Cardiolipin
(Ref. 1, pp. 164- 166)
  1. The nitrogenous base in lecithin is:
    1. Ethanolamine
    2. Choline
    3. Serine
    4. Betaine
(Ref. 1, pp. 164- 165)
  1. The nitrogenous base in cephalin is:
    1. Ethanolamine
    2. Choline
    3. Serine
    4. Betaine
(Ref. 1, pp. 164- 165)
16 B
17 C
18 C
19 A
20 C
21 B
22 C
23 B
24 A
11
  1. Hexosamines are present in:
    1. Cerebrosides
    2. Sulphatides
    3. Gangliosides
    4. Sphingosine
(Ref. 1, p. 167)
  1. All the following are omega-6 fatty acids except:
    1. Linoleic acid
    2. α-Linolenic acid
    3. γ-Linolenic acid
    4. Arachidonic acid
(Ref. 1, p. 162)
  1. Neutral fats are esters of fatty acids and:
    1. Cholesterol
    2. Glycerol
    3. Cetyl alcohol
    4. Sphingosine
(Ref. 3, p. 306)
  1. Sphingosine is not present in:
    1. Plasmalogens
    2. Cerebrosides
    3. Sulphatides
    4. Gangliosides
(Ref. 1, pp. 164-166)
  1. All the following have 18 carbon atoms except:
    1. Linoleic acid
    2. Linolenic acid
    3. Arachidonic acid
    4. Stearic acid
(Ref. 1, pp. 161-162)
  1. All the following contain nitrogen except:
    1. Lecithin
    2. Cephalin
    3. Phosphatidyl inositol
    4. Phosphatidyl serine
(Ref. 1, p. 165)
  1. The number of double bonds in linoleic acid is:
    1. 1
    2. 2
    3. 3
    4. 4
(Ref. 1, p. 162)
  1. The number of double bonds in linolenic acid is:
    1. 1
    2. 2
    3. 3
    4. 4
(Ref. 1, p. 162)
  1. The number of double bonds in arachidonic acid is:
    1. 1
    2. 2
    3. 3
    4. 4
(Ref. 1, p. 162)
25 C
26 B
27 B
28 A
29 C
30 C
31 B
32 C
33 D
12
  1. A 20-carbon fatty acid among the following is:
    1. Linoleic acid.
    2. α-Linolenic acid
    3. γ-Linolenic acid
    4. Arachidonic acid
(Ref. 1, p. 162)
  1. The following can be used as a measure of lipid peroxidation:
    1. Hydrogen peroxide
    2. Endoperoxide
    3. Hydroperoxide
    4. Malondialdehyde
(Ref. 1, p. 169)
  1. Triglycerides are transported from liver to extrahepatic tissues by:
    1. Chylomicrons
    2. VLDL
    3. HDL
    4. LDL
(Ref. 1, p. 271)
  1. Triglycerides are transported from intestines to extrahepatic tissues by:
    1. Chylomicrons
    2. VLDL
    3. HDL
    4. LDL
(Ref. 1, p. 271)
  1. Cholesterol is the precursor of:
    1. Sex hormones
    2. Vitamin D
    3. Bile acids
    4. All of the above
(Ref. 1, p. 167)
  1. Cholesterol is transported from extrahepatic tissues to liver by:
    1. Chylomicrons
    2. VLDL
    3. HDL
    4. LDL
(Ref. 1, p. 276)
  1. Elevated plasma level of the following protects against atherosclerosis:
    1. Chylomicrons
    2. VLDL
    3. HDL
    4. LDL
(Ref. 1, p. 276)
34 D
35 D
36 B
37 A
38 D
39 C
40 C

Chemistry of Amino Acids and Proteins3

  1. An amino acid having no asymmetric carbon atom is:
    1. Alanine
    2. Leucine
    3. Glycine
    4. Arginine
(Ref. 1, p. 29)
  1. An amino acid having two asymmetric carbon atoms is:
    1. Glycine
    2. Cysteine
    3. Valine
    4. Threonine
(Ref. 3, p. 99)
  1. All the following amino acids are non-essential except:
    1. Alanine
    2. Histidine
    3. Cysteine
    4. Pro line
(Ref. 1, p. 655)
  1. Sulphydryl group is present in:
    1. Cysteine
    2. Methionine
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 28)
  1. Glutathione is a:
    1. Decapeptide
    2. Octapeptide
    3. Pentapeptide
    4. Tripeptide
(Ref. 1, p. 38)
  1. Angiotensin II is a:
    1. Decapeptide
    2. Octapeptide
    3. Pentapeptide
    4. Tripeptide
(Ref. 1, p. 581)
1 C
2 D
3 B
4 A
5 D
6 B
14
  1. In quaternary structure, subunits are linked by:
    1. Peptide bonds
    2. Disulphide bonds
    3. Covalent bonds
    4. Non-covalent bonds
(Ref. 1, p. 57)
  1. High voltage electrophoresis is used to separate:
    1. Proteins
    2. Lipoproteins
    3. Amino acids
    4. All of the above
(Ref. 1, p. 42)
  1. In thin-layer chromatography, separation is based upon:
    1. Solubility
    2. Adsorption
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 34)
  1. Molecular weight of human albumin is about:
    1. 156,000
    2. 90,000
    3. 69,000
    4. 54,000
(Ref. 1, p. 738)
  1. The largest protein amongst the following is:
    1. Fibrinogen
    2. Globulin
    3. Albumin
    4. Haemoglobin
(Ref. 1, p. 738)
  1. At isoelectric pH, an amino acid exists as:
    1. Anion
    2. Cation
    3. Zwitterion
    4. None of the above
(Ref. 1, pp. 30-31)
  1. Among the following, an essential amino acid is:
    1. Phenylalanine
    2. Tyrosine
    3. Proline
    4. Hydroxyproline
(Ref. 1, p. 655)
  1. A disulphide bond can be formed between:
    1. Two methionine residues
    2. Two cysteine residues
    3. A methionine and a cysteine residue
    4. All of the above
(Ref. 1, p. 54)
7 D
8 C
9 C
10 C
11 A
12 C
13 A
14 B
15
  1. A coagulated protein is:
    1. Insoluble
    2. Biologically non-functional
    3. Unfolded
    4. All of the above
(Ref. 3, pp. 140-141)
  1. At a pH below the isoelectric point, an amino acid exists as:
    1. Cation
    2. Anion
    3. Zwitterion
    4. Undissociated molecule
(Ref. 1, pp. 30-31)
  1. If electrophoresis is carried out at pH 8.6, a protein having an isoelectric pH of 5.8 will migrate towards:
    1. Anode
    2. Cathode
    3. Either of the above
    4. Neither of the above
(Ref. 3, pp. 108, 128)
  1. The number of ionisable groups in tyrosine is:
    1. One
    2. Two
    3. Three
    4. Four
(Ref. 1, p. 29)
  1. An amino acid having a hydrophilic side chain is:
    1. Alanine
    2. Proline
    3. Methionine
    4. Serine
(Ref. 1, p. 32)
  1. An amino acid having a non-polar side chain is:
    1. Arginine
    2. Valine
    3. Glutamine
    4. Lysine
(Ref. 1, p. 32)
  1. Ultraviolet light is absorbed by:
    1. Histidine
    2. Proline
    3. Phenylalanine
    4. All of the above
(Ref. 1, p. 33)
  1. The number of peptide bonds in glutathione is:
    1. One
    2. Two
    3. Three
    4. Four
(Ref. 1, p. 38)
  1. An amino acid that does not take part in α-helix formation is:
    1. Histidine
    2. Tyrosine
    3. Proline
    4. Tryptophan
Ref 3, p. 153)
15 D
16 A
17 A
18 C
19 D
20 B
21 C
22 B
23 C
16
  1. A protein rich in cysteine is:
    1. Collagen
    2. Keratin
    3. Haemoglobin
    4. Gelatin
(Ref. 3, p. 153)
  1. A protein rich in proline is:
    1. Protamine
    2. Prothrombin
    3. Procollagen
    4. Proinsulin
(Ref. 1, pp. 60-61)
  1. Primary structure of proteins can be determined by the use of:
    1. Electrophoresis
    2. Chromatography
    3. Ninhydrin
    4. Sanger's reagent
(Ref. 1, p. 41)
  1. Primary structure of a protein is broken by:
    1. Heat
    2. Ammonium sulphate
    3. Pepsin
    4. All of the above
(Ref. 7, pp. 30, 32, 37)
  1. Electrostatic bonds can be formed between the side chains of:
    1. Alanine and leucine
    2. Leucine and valine
    3. Aspartate and glutamate
    4. Lysine and aspartate
(Ref. 1, pp. 28-29, 49)
  1. The following is a metalloprotein:
    1. Haemoglobin
    2. Myoglobin
    3. Ferritin
    4. All of the above
(Ref. 3, p. 126)
  1. Sanger's reagent contains:
    1. Phenylisothiocyanate
    2. Dansyl chloride
    3. 1-Fluoro-2, 4-dinitrobenzene
    4. Ninhydrin
(Ref. 1, p. 41)
  1. The most abundant protein in mammals is:
    1. Albumin
    2. Haemoglobin
    3. Collagen
    4. Elastin
(Ref. 1, p. 60)
24 B
25 C
26 D
27 C
28 D
29 C
30 C
31 C
17
  1. Folding of newly synthesised proteins is accelerated by:
    1. Protein disulphide isomerase
    2. Prolyl cis-trans isomerase
    3. Chaperonins
    4. All of the above
(Ref. 1, p. 59)
  1. Quaternary structure is present in:
    1. Coagulated proteins
    2. Denatured proteins
    3. Haemoglobin
    4. Myoglobin
(Ref. 1, pp. 58, 66)
  1. Primary structure of a protein is formed by:
    1. Hydrogen bonds
    2. Peptide bonds
    3. Disulphide bonds
    4. All of the above
(Ref. 1, p. 38)
  1. α-Helix is formed by:
    1. Hydrogen bonds
    2. Hydrophobic bonds
    3. Electrostatic bonds
    4. Disulphide bonds
(Ref. 1, p. 50)
  1. Glutelins are present in:
    1. Milk
    2. Eggs
    3. Meat
    4. Cereals
(Ref. 7, p. 56)
  1. β-Bends are present in:
    1. Fibrous proteins
    2. Globular proteins
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 53)
  1. Aromatic amino acids can be detected by:
    1. Sakaguchi reaction
    2. Millon-Nasse reaction
    3. Hopkins-Cole reaction
    4. Xanthoproteic reaction
(Ref. 7, pp. 34-36)
  1. Angiotensinogen is a:
    1. α1 -Globulin
    2. α2-Globulin
    3. β1 -Globulin
    4. β2-Globulin
(Ref. 1, p. 581)
32 D
33 C
34 B
35 A
36 D
37 B
38 D
39 B
18
  1. Chromatographic separation based upon differential distribution of compounds between two solvents is known as:
    1. Adsorption chromatography
    2. Partition chromatography
    3. Thin layer chromatography
    4. Column chromatography
(Ref. 1, p. 34)
  1. The number of ionisable groups in glutamate is:
    1. 1
    2. 2
    3. 3
    4. 4
(Ref. 1, p. 28)
  1. A dicarboxylic amino acid among the following is:
    1. Aspartate
    2. Lysine
    3. Arginine
    4. Tyrosine
(Ref. 1, p. 28)
  1. Two amino groups are present in:
    1. Leucine
    2. Glutamate
    3. Lysine
    4. Threonine
(Ref. 1, pp. 28-29)
  1. The least soluble protein among the following is:
    1. Albumin
    2. Globulin
    3. Casein
    4. Collagen
(Ref. 3, p. 158)
  1. During denaturation of proteins, all the following are disrupted except:
    1. Primary structure
    2. Secondary structure
    3. Tertiary structure
    4. Quaternary structure
(Ref. 1, p. 61)
  1. A branched-chain amino acid among the following is:
    1. Alanine
    2. Valine
    3. Threonine
    4. Lysine
(Ref. 1, pp. 28-29)
  1. All the following are branched chain-amino acids except:
    1. Isoleucine
    2. Alanine
    3. Leucine
    4. Valine
(Ref. 1, p. 28)
  1. All the following have aliphatic side chains except:
    1. Glycine
    2. Alanine
    3. Leucine
    4. Valine
(Ref. 1, p. 28)
40 B
41 C
42 A
43 C
44 D
45 A
46 B
47 B
48 A
19
  1. An -OH group is present in the side chain of:
    1. Serine
    2. Arginine
    3. Lysine
    4. Proline
(Ref 1, pp. 28-29)
  1. Following chromatographic separation, amino acids can be detected by:
    1. Biuret reaction
    2. Ninhydrin reaction
    3. Xanthoproteic reaction
    4. Hopkins-Cole reaction
(Ref. 1, p. 33)
  1. Edman's reagent contains:
    1. Phenylisothiocyanate
    2. 1-Fluoro-2, 4-dinitrobenzene
    3. Dansyl cphloride
    4. tBOC azide
(Ref. 1, p. 43)
  1. Edman's reaction can be used to:
    1. Determine the number of tyrosine residues in a protein
    2. Determine the number of aromatic amino acid residues in a protein
    3. Determine the amino acid sequence of a protein
    4. Hydrolyse the peptide bonds in a protein
(Ref. 1, p. 43)
  1. Presence of tyrosine can be detected by:
    1. Sakaguchi reaction
    2. Millon-Nasse reaction
    3. Hopkins-Cole reaction
    4. Biuret reaction
(Ref. 7, p. 34)
  1. Presence of arginine can be detected by:
    1. Sakaguchi reaction
    2. Millon-Nasse reaction
    3. Hopkins-Cole reaction
    4. Gas chromatography
(Ref. 7, p. 36)
  1. Plasma lipoproteins can be separated by:
    1. Salt fractionation
    2. Alcohol fractionation
    3. Ultracentrifugation
    4. Paper chromatography
(Ref. 1, p. 268)
49 A
50 B
51 A
52 C
53 B
54 A
55 C

Chemistry of Nucleotides and Nucleic Acids4

  1. An oxy group is attached to carbon number two of:
    1. Cytosine
    2. Uracil
    3. Thymine
    4. All of the above
(Ref. 1, p. 376)
  1. A methyl group is attached to carbon number five of:
    1. Adenine
    2. Guanine
    3. Thymine
    4. Cytosine
(Ref. 1, p. 376)
  1. The following nitrogen atom of purines is attached to the sugar in nucleosides:
    1. Nitrogen 1
    2. Nitrogen 3
    3. Nitrogen 7
    4. Nitrogen 9
(Ref. 1, p. 376)
  1. A nitrogenous base that does not occur in mRNA is:
    1. Cytosine
    2. Thymine
    3. Uracil
    4. All of the above
(Ref. 1, p. 376)
  1. In cyclic AMP, phosphate is attached to the following carbon atoms of ribose:
    1. 1 and 5
    2. 2 and 5
    3. 3 and 5
    4. 1 and 3
(Ref. 1, p. 381)
  1. In nucleotides, phosphate is attached to sugar by:
    1. Salt bond
    2. Hydrogen bond
    3. Ester bond
    4. Glycosidic bond
(Ref. 1, p. 378)
1 D
2 C
3 D
4 B
5 C
6 C
21
  1. Cyclic AMP can be formed from:
    1. AMP
    2. ADP
    3. ATP
    4. All of the above
(Ref. 1, p. 380)
  1. The nitrogenous base in inosine monophosphate is:
    1. Ionone
    2. Inulin
    3. Hypoxanthine
    4. Xanthine
(Ref. 1, p. 381)
  1. In some metabolic pathways, UDP is present in combination with:
    1. Glucose
    2. Glucuronic acid
    3. Galactose
    4. All of the above
(Ref. 1, pp. 224, 226)
  1. A substituted pyrimidine base of pharmacological value is:
    1. 5-Iododeoxyuridine
    2. Cytosine arabinoside
    3. 5-Fluorouracil
    4. All of the above
(Ref. 1, p. 382)
  1. A synthetic purine nucleoside of pharmacological value is:
    1. 6-Mercaptopurine
    2. 6-Thioguanine
    3. Cytosine arabinoside
    4. Adenine arabinoside
(Ref. 1, p. 382)
  1. The “transforming factor” discovered by Avery, McLeod and McCarty was later found to be:
    1. mRNA
    2. tRNA
    3. DNA
    4. None of the above
(Ref. 1, p. 402)
  1. In DNA, the complementary base of adenine is:
    1. Guanine
    2. Cytosine
    3. Uracil
    4. Thymine
(Ref. 1, p. 402)
  1. In DNA, three hydrogen bonds are formed between:
    1. Adenine and guanine
    2. Adenine and thymine
    3. Guanine and cytosine
    4. Thymine and cytosine
(Ref. 1, p. 403)
7 C
8 C
9 D
10 C
11 D
12 C
13 D
14 C
22
  1. The diameter of the double helix is 2 nm in:
    1. A-DNA
    2. B-DNA
    3. Z-DNA
    4. None of the above
(Ref. 1, p. 403)
  1. Twelve base pairs are present in each turn of the helix in:
    1. A-DNA
    2. B-DNA
    3. Z-DNA
    4. None of the above
(Ref. 2, p. 791)
  1. Alternate purine and pyrimidine bases are present in:
    1. A-DNA
    2. B-DNA
    3. Z-DNA
    4. None of the above
(Ref. 2, p. 791)
  1. Left-handed double helix is present in:
    1. Z-DNA
    2. A-DNA
    3. B-DNA
    4. None of the above
(Ref. 2, p. 791)
  1. Right-handed double helix is present in:
    1. A-DNA and Z-DNA
    2. B-DNA and Z-DNA
    3. A-DNA and B-DNA
    4. All the three pairs
(Ref. 2, p. 791)
  1. Nuclear DNA is present in combination with:
    1. Histones
    2. Non-histones
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 412)
  1. The pyrimidine bases in RNA are:
    1. Cytosine and uracil
    2. Cytosine and thymine
    3. Thymine and uracil
    4. Any of these pairs
(Ref. 1, p. 376)
  1. Number of guanine and cytosine residues is equal in:
    1. mRNA
    2. tRNA
    3. DNA
    4. None of the above
(Ref. 1, p. 402)
15 B
16 C
17 C
18 A
19 C
20 C
21 A
22 C
23
  1. Alkalis can not hydrolyse:
    1. mRNA
    2. tRNA
    3. rRNA
    4. DNA
(Ref. 1, p. 406)
  1. 7-Methylguanosine triphosphate cap is present at the:
    1. 5'-End of tRNA
    2. 3'-End of tRNA
    3. 5'-End of mRNA
    4. 3'-End of mRNA
(Ref. 1, pp. 407-408)
  1. Poly-A tail is present at:
    1. 5'-End of mRNA
    2. 3'-End of mRNA
    3. 5'-End of tRNA
    4. 3'-End of tRNA
(Ref. 1, p. 408)
  1. Heterogeneous nuclear RNA is the precursor of:
    1. mRNA
    2. tRNA
    3. rRNA
    4. All of the above
(Ref. 1, p. 408)
  1. Codons are present in:
    1. Template strand of DNA
    2. mRNA
    3. tRNA
    4. rRNA
(Ref. 1, pp. 435, 453)
  1. Amino acid is attached to tRNA at:
    1. 5'-End
    2. 3'-End
    3. Anticodon
    4. DHU loop
(Ref. 1, p. 410)
  1. The terminal nucleotide sequence is CCA at the:
    1. 5'-End of tRNA
    2. 3'-End of tRNA
    3. 5'-End of mRNA
    4. 3'-End of mRNA
(Ref. 1, p. 410)
  1. In eukaryotes, 40 S and 60 S subunits of ribosomes combine to form:
    1. 70 S ribosomes
    2. 80 S ribosomes
    3. 100 S ribosomes
    4. None of the above
(Ref. 1, p. 410)
  1. In prokaryotes, the ribosomal subunits are:
    1. 30 S and 40 S
    2. 40 S and 50 S
    3. 30 S and 50 S
    4. 40 S and 60 S
(Ref. 2, p. 907)
23 D
24 C
25 B
26 A
27 B
28 B
29 B
30 B
31 C
24
  1. A nucleotide that forms a high-energy intermediate for lipid synthesis is:
    1. ADP
    2. GDP
    3. UDP
    4. CDP
(Ref. 1, p.375)
  1. A purine base is present in all the following coenzymes except:
    1. NAD
    2. NADP
    3. FMN
    4. FAD
(Ref. 1, p.375)
  1. The smallest RNA amongst the following is:
    1. rRNA
    2. hnRNA
    3. mRNA
    4. tRNA
(Ref. 1, p. 411)
  1. The largest RNA amongst the following is:
    1. rRNA
    2. hnRNA
    3. mRNA
    4. tRNA
(Ref. 1, pp. 408-411)
  1. The number of adenine and thymine bases is equal in:
    1. DNA
    2. mRNA
    3. tRNA
    4. rRNA
(Ref. 1, pp. 402, 406)
  1. The number of purine bases and pyrimidine bases is equal in:
    1. DNA
    2. mRNA
    3. tRNA
    4. rRNA
(Ref. 1, pp. 402, 406)
  1. The number of hydrogen bonds between adenine and thymine in DNA is:
    1. One
    2. Two
    3. Three
    4. Four
(Ref. 1, p. 403)
32 D
33 C
34 D
35 B
36 A
37 A
38 B
25
  1. The complementary base of adenine in RNA is:
    1. Thymine
    2. Cytosine
    3. Guanine
    4. Uracil
(Ref. 1, p. 408)
  1. Pseudouridine is present in:
    1. hnRNA
    2. mRNA
    3. tRNA
    4. rRNA
(Ref. 1, p. 398)
  1. Dihydrouracil is present in:
    1. hnRNA
    2. mRNA
    3. tRNA
    4. rRNA
(Ref. 1, p.410)
  1. The number of nucleotides in a tRNA molecule is about:
    1. 25
    2. 50
    3. 75
    4. 200
(Ref. 1, p. 411)
  1. 60 S ribosomal subunit contains all the following except:
    1. 5 S rRNA
    2. 5.8 S rRNA
    3. 18 S rRNA
    4. 28 S rRNA
(Ref. 1, p. 410)
  1. Extranuclear DNA is present in:
    1. Ribosomes
    2. Endoplasmic reticulum
    3. Lysosomes
    4. Mitochondria
(Ref. 2, p. 988)
  1. Extranuclear DNA:
    1. Doesn't encode proteins
    2. Encodes proteins which are used in ribosomes
    3. Encodes proteins which are used in mitochondria
    4. Encodes proteins which can be used anywhere in the cell
(Ref. 1, p. 837)
  1. Mitochondrial DNA is present in:
    1. Bacteria
    2. Viruses
    3. Eukaryotes
    4. All of the above
(Ref. 2, p. 988)
  1. The following is synthesised in the form of a large precursor in eukaryotes:
    1. tRNA
    2. rRNA
    3. mRNA
    4. All of the above
(Ref. 1, p. 448)
39 D
40 C
41 C
42 C
43 C
44 D
45 C
46 C
47 D
26
  1. Ribothymidine is present in:
    1. DNA
    2. tRNA
    3. rRNA
    4. hnRNA
(Ref. 1, p. 410)
  1. DNA contains all the following except:
    1. Adenine
    2. Thiamin
    3. Cytosine
    4. Guanine
(Ref. 1, p. 402)
  1. Hypoxanthine may be present in:
    1. DNA
    2. mRNA
    3. tRNA
    4. rRNA
(Ref. 1, p. 454)
  1. DHU loop is present in:
    1. hnRNA
    2. mRNA
    3. tRNA
    4. rRNA
(Ref. 2, p. 878)
  1. The only correct statement about pseudouridine is:
    1. It is present in rRNA
    2. It contains dihydrouracil
    3. It contains deoxyribose
    4. The base and sugar are joined by C—C bond
(Ref. 3, p. 876)
  1. Ten base pairs are present in one turn of the helix in:
    1. A-DNA
    2. B-DNA
    3. C-DNA
    4. Z-DNA
(Ref. 2, pp. 788, 791)
  1. Double helical DNA is unwound on:
    1. Raising the temperature
    2. Lowering the temperature
    3. Exposure to X-rays
    4. Exposure to gamma radiation
(Ref. 1, p. 404)
  1. Transfer RNA transfers:
    1. Information from DNA to ribosomes
    2. Information from mRNA to cytosol
    3. Amino acids from cytosol to ribosomes
    4. Proteins from ribosomes to cytosol
(Ref. 2, p. 102)
48 B
49 B
50 C
51 C
52 D
53 B
54 A
55 C

Enzymes5

  1. The following is a group-specific enzyme:
    1. Pepsin
    2. Aminopeptidase
    3. Phospholipase D
    4. All of the above
(Ref. 1, pp. 263, 663, 665)
  1. The following is a substrate-specific enzyme:
    1. Hexokinase
    2. Thiokinase
    3. Lactase
    4. Aminopeptidase
(Ref. 1, pp. 191, 238, 669)
  1. The following is not a substrate-specific enzyme:
    1. Glucokinase
    2. Fructokinse
    3. Hexokinase
    4. Phosphofructokinase
(Ref. 1, pp. 191, 225)
  1. Chymotrypsin hydrolyses peptide bonds in which carboxyl group is contributed by:
    1. Phenylalanine
    2. Tyrosine
    3. Tryptophan
    4. Any of the above
(Ref. 1, p. 664)
  1. Coenzymes combine with:
    1. Proenzymes
    2. Apoenzymes
    3. Holoenzymes
    4. Antienzymes
(Ref. 3, p. 209)
  1. Coenzymes are required in the following reactions:
    1. Oxidation-reduction
    2. Transamination
    3. Phosphorylation
    4. All of the above
(Ref. 1, p. 75)
1 D
2 C
3 C
4 D
5 B
6 D
28
  1. The following coenzyme takes part in hydrogen transfer reactions:
    1. Tetrahydrofolate
    2. Coenzyme A
    3. Coenzyme Q
    4. Biotin
(Ref. 1, p. 76)
  1. The following coenzyme does not take part in hydrogen transfer reactions:
    1. FAD
    2. NMD
    3. NADP
    4. Cobamides
(Ref. 1, p. 76)
  1. The following coenzyme takes part in oxidation reduction reactions:
    1. Pyridoxal phosphate
    2. Lipoic acid
    3. Thiamin diphosphate
    4. None of the above
(Ref. 1, p. 76)
  1. In conversion of glucose to glucose-6-phosphate, the coenzyme is:
    1. Mg ++
    2. ATP
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 191)
  1. A coenzyme required in transamination reactions is:
    1. Coenzyme A
    2. Coenzyme Q
    3. Biotin
    4. Pyridoxal phosphate
(Ref. 1, p. 633)
  1. A coenzyme required in the transfer of single carbon moieties is:
    1. Lipoic acid
    2. Coenzyme A
    3. Pyridoxal phosphate
    4. Tetrahydrofolate
(Ref. 1, p. 638)
  1. Coenzyme A contains a vitamin which is:
    1. Thiamin
    2. Ascorbic acid
    3. Pantothenic acid
    4. Niacinamide
(Ref. 1, p. 632)
7 C
8 D
9 B
10 B
11 D
12 D
13 C
29
  1. Cobamides contain a vitamin which is:
    1. Folic acid
    2. Ascorbic acid
    3. Pantothenic acid
    4. Vitamin B12
(Ref. 1, p. 76)
  1. A coenzyme required in carboxylation reactions is:
    1. Lipoic acid
    2. Coenzyme A
    3. Biotin
    4. All of the above
(Ref. 1, p. 634)
  1. Pyridoxal phosphate acts as a coenzyme for:
    1. Alanine aminotransferase
    2. Aspartate aminotransferase
    3. Tyrosine aminotransferase
    4. All of the above
(Ref. 1, pp. 315, 325, 333)
  1. The following coenzyme takes part in tissue respiration:
    1. Coenzyme Q
    2. Coenzyme A
    3. NADP
    4. Cobamide
(Ref. 1, p. 139)
  1. The enzyme hexokinase is a:
    1. Hydrolase
    2. Oxidoreductase
    3. Transferase
    4. Ligase
(Ref. 1, p. 75)
  1. The following enzyme is a hydrolase:
    1. Aldolase
    2. Enolase
    3. Fumarase
    4. Amylase
(Ref. 1, pp. 74, 186, 191, 194)
  1. The following is a proteolytic enzyme:
    1. Pepsin
    2. Trypsin
    3. Chymotrypsin
    4. All of the above
(Ref. 1, p. 668)
  1. The following enzyme is a lyase:
    1. Fumarase
    2. Amylase
    3. Maltase
    4. Invertase
(Ref. 6, p. 38)
14 D
15 C
16 D
17 A
18 C
19 D
20 D
21 A
30
  1. The following enzyme has no optical specificity:
    1. Triose phosphate isomerase
    2. Phosphohexose isomerase
    3. Alanine racemase
    4. All of the above
(Ref. 1, p. 77)
  1. Pyridoxal phosphate acts as a coenzyme for:
    1. GOT
    2. Tyrosine transaminase
    3. Phosphorylase
    4. All of the above
(Ref. 1, pp. 633-634)
  1. Enzymes which catalyse binding of two substrates by covalent bonds are known as:
    1. Lyases
    2. Hydrolases
    3. Ligases
    4. Oxidoreductases
(Ref. 6, p. 38)
  1. The induced fit model of enzyme action was proposed by:
    1. Fischer
    2. Koshland
    3. Mitchell
    4. Markert
(Ref. 1, p. 91)
  1. Allosteric inhibition is also known as:
    1. Competitive inhibition
    2. Non-competitive inhibition
    3. Feedback inhibition
    4. None of the above
(Ref. 1, p. 115)
  1. An allosteric enzyme:
    1. Is generally present at the end of a pathway
    2. Generally catalyses a reversible reaction
    3. Generally catalyses the committed step unique to a pathway
    4. Possesses only substrate site
(Ref. 1, p. 115)
  1. An allosteric enzyme is generally inhibited by:
    1. Initial substrate of the pathway
    2. Substrate analogues
    3. Product of the reaction catalysed by allosteric enzyme
    4. Product of the pathway
(Ref. 1, p. 115)
22 C
23 D
24 C
25 B
26 C
27 C
28 D
31
  1. When the substrate concentration equals Km in an enzyme-catalysed reaction:
    1. A few of the enzyme molecules are present as ES complex
    2. Majority of the enzyme molecules are present as ES complex
    3. Half of the enzyme molecules are present as ES complex
    4. All the enzyme molecules are present as ES complex
(Ref. 1, p. 95)
  1. When the velocity of an enzymatic reaction equals Vmax, substrate concentration is:
    1. Half of Km
    2. Equal to Km
    3. Twice the Km
    4. Far above the Km
(Ref. 1, p. 95)
  1. When the velocity of an enzymatic reaction is half of Vmax:
    1. Substrate concentration is half of Km
    2. Substrate concentration is equal to Km
    3. Substrate concentration is twice the Km
    4. None of the above
(Ref. 1, p. 95)
  1. In Lineweaver-Burk plot, the y-intercept represents:
    1. Vmax
    2. 1/Vmax
    3. Km
    4. 1/Km
(Ref. 1, p. 96)
  1. In Lineweaver-Burk plot, the x-intercept represents:
    1. Vmax
    2. Km
    3. Reciprocal of Vmax
    4. Reciprocal of Km
(Ref. 1, p. 96)
  1. In competitive inhibition, the inhibitor:
    1. Competes with the enzyme
    2. Irreversibly binds with the enzyme
    3. Binds with the substrate
    4. Competes with the substrate
(Ref. 1, p. 98)
29 C
30 D
31 B
32 B
33 D
34 D
32
  1. A competitive inhibitor:
    1. Bears a structural resemblance with the enzyme
    2. Bears a structural resemblance with the substrate
    3. Combines with the enzyme at the allosteric site
    4. Combines with the substrate and prevents it from binding with the enzyme (Ref. 1, p. 98)
  1. Competitive inhibitors:
    1. Decrease the Km
    2. Decrease the Vmax
    3. Increase the Km
    4. Increase the Vmax
(Ref. 1, p. 99)
  1. Competitive inhibition can be relieved by raising the:
    1. Enzyme concentration
    2. Substrate concentration
    3. Inhibitor concentration
    4. None of the above
(Ref. 1, p. 98)
  1. Acetylcholinesterase is competitively inhibited by:
    1. Aminopterin
    2. Acetylcholine
    3. Neostigmine
    4. Allopurinol
(Ref. 1, p. 832)
  1. Pyridostigmine is a competitive inhibitor of:
    1. Xanthine oxidase
    2. Acetylcholinesterase
    3. Carbonic anhydrase
    4. Monoamine oxidase
(Ref. 1, p. 832)
  1. Dihydrofolate reductase is competitively inhibited by:
    1. Allopurinol
    2. Neostigmine
    3. Acetazolamide
    4. Methotrexate
(Ref. 1, pp. 638-639)
  1. Carbonic anhydrase is competitively inhibited by:
    1. Allopurinol
    2. Acetazolamide
    3. Aminopterin
    4. Neostigmine
(Ref. 3, p. 247)
  1. Allopurinol is a competitive inhibitor of:
    1. Dihydrofolate reductase
    2. Xanthine oxidase
    3. Carbonic anhydrase
    4. Acetylcholinesterase
(Ref. 1, p. 382)
35 B
36 C
37 B
38 C
39 B
40 D
41 B
42 B
33
  1. Non-competitive inhibitors:
    1. Increase the Km
    2. Increase the Vmax
    3. Decrease the Km
    4. Decrease the Vmax
(Ref. 1, p. 99)
  1. Non-competitive inhibitors:
    1. Resemble the substrate in structure
    2. Resemble the substrate site in structure
    3. Bind with the enzyme at the allosteric site
    4. None of the above
(Ref. 1, p. 99)
  1. Serum lactate dehydrogenase rises in:
    1. Viral hepatitis
    2. Myocardial infarction
    3. Carcinomatosis
    4. All of the above
(Ref. 1, p. 83)
  1. The following serum enzyme rises in viral hepatitis:
    1. LDH
    2. GPT
    3. GGT
    4. All of the above
(Ref. 1, p. 83)
  1. The following serum enzyme rises in myocardial infarction:
    1. Creatine kinase
    2. GOT
    3. LDH
    4. All of the above
(Ref. 1, p. 83)
  1. Following myocardial infarction, the earliest serum enzyme to rise is:
    1. Creatine kinase
    2. GOT
    3. GPT
    4. LDH
(Ref. 6, p. 55)
  1. Creatine kinase is found in:
    1. Myocardium
    2. Brain
    3. Muscles
    4. All of the above
(Ref. 6, p. 56)
  1. Following myocardial infarction, the last serum enzyme to return to normal is:
    1. Creatine kinase
    2. GOT
    3. GPT
    4. LDH
(Ref. 6, p. 55)
43 D
44 D
45 D
46 D
47 D
48 A
49 D
50 D
34
  1. In viral hepatitis:
    1. The rise in SGOT is greater than that in SGPT
    2. The rise in SGPT is greater than that in SGOT
    3. SGOT and SGPT are raised equally
    4. SGOT remains normal
(Ref. 1, p. 83)
  1. The highest elevation in serum alkaline phosphatase is seen in:
    1. Obstructive jaundice
    2. Rickets
    3. Osteomalacia
    4. Infective hepatitis
(Ref. 1, p. 83)
  1. Alkaline phosphatase is present in:
    1. Liver
    2. Bones
    3. Placenta
    4. All of the above
(Ref. 6, p. 57)
  1. Serum lipase is raised in:
    1. Acute pancreatitis
    2. Acute parotitis
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 83)
  1. Serum acid phosphatase is raised in:
    1. Cancer of liver
    2. Cancer of bones
    3. Cancer of prostate
    4. All of the above
(Ref. 1, p. 83)
  1. Serum amylase is raised in:
    1. Acute pancreatitis
    2. Infective hepatitis
    3. Obstructive jaundice
    4. None of the above
(Ref. 1, p. 83)
  1. The following isoenzyme of lactate dehydrogenase is raised in serum in myocardial infarction:
    1. LD1
    2. LD2
    3. LD1 and LD2
    4. LD5
(Ref. 1, p. 82)
  1. The subunit composition of LD1, isoenzyme of lactate dehydrogenase is:
    1. HHHH
    2. HHHM
    3. HMMM
    4. MMMM
(Ref. 1, p. 82)
51 B
52 A
53 D
54 A
55 C
56 A
57 C
58 A
35
  1. The following isoenzyme of creatine kinase in serum is raised in myocardial infarction:
    1. CK-BB
    2. CK-MM
    3. CK-MB
    4. All of the above
(Ref. 1, p. 854)
  1. The following isoenzyme of creatine kinase in serum is raised in myopathies:
    1. CK-BB
    2. CK-MM
    3. CK-MB
    4. None of the above
(Ref. 6, p. 56)
  1. Enzymes which are always present in an organism are known as:
    1. Inducible enzymes
    2. Constitutive enzymes
    3. Functional enzymes
    4. Apoenzymes
(Ref. 1, p. 114)
  1. Enzyme synthesis is repressed when:
    1. Aporepressor is present in the cell
    2. Inducer is absent from the cell
    3. Inducer is absent and aporepressor present in the cell
    4. Aporepressor and corepressor are present in the cell
(Ref. 1, pp. 361, 365)
  1. Inactive precursors of enzymes are known as:
    1. Apoenzymes
    2. Coenzymes
    3. Proenzymes
    4. Holoenzymes
(Ref. 1, p. 118)
  1. The following is a proenzyme:
    1. Carboxypeptidase
    2. Aminopeptidase
    3. Chymotrypsin
    4. Pepsinogen
(Ref. 1, pp. 668-669)
  1. Allosteric enzymes may undergo:
    1. Feedback inhibition
    2. Covalent modification
    3. Repression
    4. Induction
(Ref. 1, p.117)
59 C
60 B
61 B
62 D
63 C
64 D
65 A
36
  1. Regulation of some enzymes by covalent modification involves addition or removal of:
    1. Acetate
    2. Sulphate
    3. Phosphate
    4. Coenzyme A
(Ref. 1, p. 119)
  1. In case of enzymes regulated by covalent modification, addition of phosphate to the enzyme converts:
    1. Inactive enzyme into active enzyme
    2. Active enzyme into inactive enzyme
    3. Either A or B
    4. Neither A nor B
(Ref. 1, p. 120)
  1. Phosphorylation of an enzyme:
    1. Alters gene expression
    2. Occurs at catalytic site
    3. Requires a repressor
    4. Is reversible
(Ref. 1, p. 120)
  1. An inorganic ion required for the activity of an enzyme is known as:
    1. Activator
    2. Cofactor
    3. Coenzyme
    4. None of the above
(Ref. 3, p. 209)
  1. The first enzyme found to have isoenzymes was:
    1. Alkaline phosphatase
    2. Lactate dehydrogenase
    3. Acid phosphatase
    4. Creatine kinase
(Ref. 3, p. 140)
  1. An allosteric inhibitor may:
    1. Raise the Km
    2. Lower the Vmax
    3. Neither of the above
    4. Either of the above
(Ref. 1, p.117)
  1. Prostatic acid phosphatase is inhibited by:
    1. Inorganic phosphate
    2. Phosphate esters
    3. Tartarate
    4. Fructose
(Ref. 3, p. 246)
  1. Lactate dehydrogenase is located in:
    1. Lysosomes
    2. Mitochondria
    3. Cytosol
    4. Microsomes
(Ref. 1, p. 191)
66 C
67 C
68 D
69 B
70 B
71 D
72 C
73 C
37
  1. Lactate dehydrogenase is a:
    1. Monomer
    2. Dimer
    3. Tetramer
    4. Hexamer
(Ref. 1, p. 82)
  1. Isoenzymes of lactate dehydrogenase:
    1. Catalyse the same reaction
    2. Have the same subunit composition
    3. Have the same electrophoretic mobility
    4. Have the same Km
(Ref. 1, pp. 81-82)
  1. Serum gamma glutamyl transpeptidase is raised in:
    1. Liver diseases
    2. Pancreatic diseases
    3. Myopathies
    4. Brain diseases
(Ref. 1, p. 83)
  1. Hepatic copper-binding P-type ATPase is defective in:
    1. Cirrhosis of liver
    2. Wilson's disease
    3. Menkes' disease
    4. Copper deficiency
(Ref. 1, p. 744)
  1. Ceruloplasmin oxidises:
    1. Copper
    2. Iron
    3. Both of the above
    4. Neither of the above
(Ref. 6, p. 30)
  1. After myocardial infarction, peak elevation of serum LDH is likely at:
    1. 12 hrs
    2. 24 hrs
    3. 3 days
    4. 7 days
(Ref. 6, p. 55)
  1. After myocardial infarction, peak elevation of serum creatine kinase is likely at:
    1. 3 hrs
    2. 6 hrs
    3. 12 hrs
    4. 24 hrs
(Ref. 6, p. 55)
  1. Following myocardial infarction, serum creatine kinase returns to normal in about:
    1. 24 hrs
    2. 3 days
    3. 5 days
    4. 7 days
(Ref. 6, p. 55)
  1. Following myocardial infarction, serum LDH returns to normal in about:
    1. 24 hrs
    2. 3 days
    3. 5 days
    4. 7 days
(Ref. 6, p. 55)
74 C
75 A
76 A
77 B
78 B
79 C
80 D
81 B
82 D
38
  1. Creatine kinase is present in all of the following except:
    1. Liver
    2. Myocardium
    3. Muscles
    4. Brain
(Ref. 6, p. 55)
  1. Serum lactate dehydrogenase may be raised in:
    1. Gilbert's disease
    2. Hepatocellular jaundice
    3. Obstructive jaundice
    4. All of the above
(Ref. 6, p. 55)
  1. Alkaline phosphatase is present in:
    1. Liver
    2. Bones
    3. Intestinal mucosa
    4. All of the above
(Ref. 6, p. 57)
  1. All the following statements about alkaline phosphatase are true except:
    1. It is substrate-specific
    2. It removes inorganic phosphate from the substrate
    3. Its optimum pH is in the basic range
    4. It requires an inorganic cofactor
(Ref. 6, p. 57)
  1. All the following are zinc-containing enzymes except:
    1. Acid phosphatase
    2. Alkaline phosphatase
    3. Carbonic anhydrase
    4. RNA polymerase
(Ref. 6, p. 440)
  1. Magnesium ions are cofactors for all the following except:
    1. Hexokinase
    2. Pyruvate kinase
    3. PEP carboxykinase
    4. Lactate dehydrogenase
(Ref. 2, pp. 445, 571, 577)
  1. All the following are iron-containing enzymes except:
    1. Carbonic anhydrase
    2. Catalase
    3. Peroxidase
    4. Cytochrome oxidase
(Ref. 6, p. 435)
  1. Biotin is a coenzyme for:
    1. Pyruvate dehydrogenase
    2. Pyruvate carboxylase
    3. PEP carboxykinase
    4. Glutamate pyruvate transaminase
(Ref. 1, pp. 634-635)
83 A
84 B
85 D
86 A
87 A
88 D
89 A
90 B
39
  1. Enzymes accelerate the rate of reactions by:
    1. Increasing the equilibrium constant of reactions
    2. Increasing the energy of activation
    3. Decreasing the energy of activation
    4. Decreasing the free energy change of the reaction
(Ref. 2, p. 188)
  1. Binding of the allosteric inhibitor to the allosteric enzyme is:
    1. Covalent
    2. Reversible
    3. Energy-consuming
    4. All of the above
(Ref. 1, p. 115)
  1. Kinetics of allosteric inhibition may be:
    1. Competitive
    2. Non-competitive
    3. Partially competitive
    4. Any of the above
(Ref. 1, p. 115)
  1. Allosteric enzymes have all the following properties except:
    1. They are under hormonal control
    2. Enzyme inhibitor binding is reversible
    3. They provide for short-term control
    4. They generally catalyse keep in early reaction in a long pathway
(Ref. 1, pp. 120-121)
  1. Covalent modification of an enzyme usually involves phosphorylation/dephosphorylation of:
    1. Serine residue
    2. Proline residue
    3. Hydroxyproline residue
    4. Hydroxylysine residue
(Ref. 1, p. 119)
  1. Vmax of an enzyme may be affected by:
    1. pH
    2. Temperature
    3. Non-competitive inhibitors
    4. All of the above
(Ref. 1, pp. 93, 99)
91 C
92 B
93 D
94 A
95 A
96 D
40
  1. In enzyme assays, all the following are kept constant except:
    1. Substrate concentration
    2. Enzyme concentration
    3. pH
    4. Temperature
(Ref. 3, pp. 218-219)
  1. If the substrate concentration is much below the Km of the enzyme, the velocity of the reaction is:
    1. Directly proportional to substrate concentration
    2. Not affected by enzyme concentration
    3. Nearly equal to Vmax
    4. Inversely proportional to substrate concentration
(Ref. 1, p. 95)
  1. Covalent modification and allosteric regulation have all the following similarities except:
    1. Both affect catalytic efficiency
    2. Neither alters gene expression
    3. Both are under hormonal control
    4. Both are short-term
(Ref. 1, pp. 120-121)
  1. In enzyme assays, pH and temperature are kept constant and:
    1. Substrate concentration is kept very low so that velocity remains proportional to substrate concentration
    2. Substrate concentration is kept very low so that velocity remains proportional to enzyme concentration
    3. Substrate concentration is kept very high so that velocity remains proportional to enzyme concentration
    4. Products are constantly removed to prevent backward reaction
(Ref. 3, pp. 218-219)
  1. Enzymes requiring NAD as a co-substrate can be assayed by measuring change in absorbance at:
    1. 210 nm
    2. 290 nm
    3. 340 nm
    4. 365 nm
(Ref. 1, p. 77)
97 B
98 A
99 C
100 C
101 C
41
  1. Different isoenzymes of an enzyme have the same:
    1. Amino acid sequence
    2. Michaelis constant
    3. Catalytic activity
    4. All of the above
(Ref. 1, pp. 81-82)
  1. Biotin is bound to:
    1. Lysine residues of carboxylases
    2. Lysine residues of decarboxylases
    3. Serine residues of carboxylases
    4. Serine residues of decarboxylases
(Ref. 3, p. 259)
  1. From the pentapeptide, phe-ala-leu-lys-arg, phenylalanine residue is split off by:
    1. Trypsin
    2. Chymotrypsin
    3. Aminopeptidase
    4. Carboxypeptidase
(Ref. 1, p. 665)
  1. From the pentapeptide, phe-ala-leu-lys-arg, arginine residue is split off by:
    1. Trypsin
    2. Chymotrypsin
    3. Aminopeptidase
    4. Carboxypeptidase
(Ref. 1, p. 664)

Biological Oxidation6

  1. A high-energy phosphate amongst the following is:
    1. Glucose-6-phosphate
    2. Glucose-1-phosphate
    3. 1,3-Biphosphoglycerate
    4. All of the above
(Ref. 1, p. 126)
  1. ADP can receive a phosphate group from:
    1. Fructose-6-phosphate
    2. Glycerol-3-phosphate
    3. Creatine phosphate
    4. None of the above
(Ref. 1, p. 126)
  1. The highest group transfer potential is present amongst the following in:
    1. 1,3-Biphosphoglycerate
    2. Creatine phosphate
    3. Carbamoyl phosphate
    4. Phosphoenol pyruvate
(Ref. 1, p. 126)
  1. The following reaction can be considered as oxidation:
    1. Fe+++ + electron → Fe++
    2. Cu++ + electron → Cu+
    3. Fe++ → Fe+++ + electron
    4. None of the above
(Ref. 1, p. 130)
  1. The compound having the lowest redox potential amongst the following is:
    1. Hydrogen
    2. NAB
    3. Cytochrome b
    4. Cytochrome a
(Ref. 1, p. 131)
1 C
2 C
3 D
4 C
5 A
43
  1. The compound having the highest redox potential amongst the following is:
    1. Coenzyme Q
    2. NAD
    3. Cytochrome c
    4. Cytochrome b
(Ref. 1, p. 131)
  1. Standard free energy of hydrolysis of ATP into ADP and Pi is:
    1. − 7.3 kcal / mol
    2. + 7.3 kcal / mol
    3. − 6.6 kcal / mol
    4. + 6.6 kcal / mol
(Ref. 1, p.126)
  1. Cytochrome oxidase is poisoned by all the following except:
    1. Carbon monoxide
    2. Hydrogen sulphide
    3. Oligomycin
    4. Cyanide
(Ref. 1, pp. 131, 141)
  1. L-Amino acid oxidase contains:
    1. FAD
    2. FMN
    3. NADP
    4. NAD
(Ref. 1, p.131)
  1. All the following statements about L-amino acid oxidase are true except:
    1. It is a flavoprotein
    2. It transfers hydrogen atoms from its substrate to oxygen forming water
    3. It contains FMN as prosthetic group
    4. Its prosthetic group is bound tightly to the apoenzyme protein
(Ref. 1, p.131)
  1. Iron-porphyrin is present as prosthetic group in:
    1. Cytochromes
    2. Catalase
    3. Peroxidase
    4. All of the above
(Ref. 1, p. 133)
  1. Enzymes which incorporate oxygen into a substrate are called:
    1. Oxidases
    2. Dehydrogenases
    3. Oxygenases
    4. Hydroperoxidases
(Ref. 1, p.134)
6 C
7 A
8 C
9 B
10 B
11 D
12 C
44
  1. Microsomal hydroxylase system contains a:
    1. Di-oxygenase
    2. Mono-oxygenase
    3. Oxidase
    4. Hydroperoxidase
(Ref. 1, p.134)
  1. A cytochrome present in microsomal hydroxylase system is:
    1. Cytochrome a
    2. Cytochrome b
    3. Cytochrome a3
    4. None of the above
(Ref. 1, p. 134)
  1. Superoxide radicals can be detoxified by:
    1. Cytochrome c
    2. Cytochrome b
    3. Cytochrome a
    4. None of the above
(Ref. 1, p. 135)
  1. A copper-containing cytochrome is:
    1. Cytochrome a
    2. Cytochrome P-450
    3. Cytochrome a3
    4. None of the above
(Ref. 1, pp. 131, 135)
  1. At sites of phosphorylation in the respiratory chain, the minimum difference in the redox potentials of two consecutive components is:
    1. 0.2 millivolts
    2. 0.2 volts
    3. 0.42 millivolts
    4. 0.42 volts
(Ref. 2, p. 548)
  1. When reducing equivalents enter the respiratory chain through NAD, the P:O ratio is:
    1. 1:2
    2. 2:1
    3. 1:3
    4. 3:1
(Ref. 1, p. 141)
  1. Rate of tissue respiration is raised when the intracellular concentration of:
    1. ADP increases
    2. ATP increases
    3. ADP decreases
    4. None of the above
(Ref. 1, p. 141)
  1. Cyanide inhibits phosphorylation at:
    1. Site I
    2. Site II
    3. Site III
    4. None of the above
(Ref. 6, p. 261)
13 B
14 D
15 A
16 C
17 B
180
19 A
20 C
45
  1. The following component of respiratory chain is not fixed in the inner mitochondrial membrane:
    1. Coenzyme Q
    2. Cytochrome c
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 140)
  1. F0 component of vectorial ATP synthetase is inhibited by:
    1. Dinitrophenol
    2. Rotenone
    3. Cyanide
    4. Oligomycin
(Ref. 2, p. 546)
  1. Uncouplers of oxidative phosphorylation:
    1. Inhibit F0 component of vectorial ATP synthetase
    2. Inhibit F1 component of vectorial ATP synthetase
    3. Make the inner mitochondrial membrane permeable to H+
    4. Inactivate cytochromes
(Ref. 1, p. 145)
  1. Extramitochondrial NADH can be oxidised in the respiratory chain with the help of:
    1. Glycerophosphate shuttle
    2. Malate shuttle
    3. Either of the above
    4. Neither of the above
(Ref. 1, p. 146)
  1. In some reactions, energy is captured in the form of:
    1. GTP
    2. UTP
    3. CTP
    4. None of the above
(Ref. 2, p. 511)
  1. Substrate-linked phosphorylation occurs in:
    1. Glycolytic pathway
    2. Citric acid cycle
    3. Both of the above
    4. Neither of the above
(Ref. 1, pp. 186, 194)
  1. Reducing equivalents move in the respiratory chain from:
    1. Relatively electronegative to electropositive components
    2. Lower redox potential to higher redox potential
    3. Reduced substrate to oxygen
    4. All of the above
(Ref. 1, pp. 137, 138)
21 C
22 D
23 C
24 C
25 A
26 C
27 D
46
  1. Hydrogen peroxide may be detoxified in the absence of an oxygen acceptor by:
    1. Peroxidase
    2. Catalase
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 133)
  1. All the following statements about hepatic microsomal hydroxylase system are correct except:
    1. It metabolises several drugs
    2. It contains cytochrome P-450
    3. It contains a flavoprotein
    4. It contains iron-sulphur protein
(Ref. 1, pp.134-135)
  1. Superoxide radicals can be detoxified by:
    1. Cytochrome c
    2. Superoxide dismutase
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 135)
28 B
29 D
30 C

Water-soluble Vitamins7

  1. Deficiencies of water-soluble vitamins can cause all of the following except:
    1. Rickets
    2. Beriberi
    3. Pellagra
    4. Scurvy
(Ref. 1, p.627)
  1. Thiamin diphosphate acts as a coenzyme for:
    1. Aldolase
    2. Transaldolase
    3. Transketolase
    4. All of the above
(Ref. 1, pp. 627-628)
  1. Thiamin diphosphate is required as a coenzyme in:
    1. HMP Shunt
    2. Citric acid cycle
    3. Both of the above
    4. Neither of the above
(Ref. 1, pp. 184, 221)
  1. Thiamin diphosphate is required for oxidative decarboxylation of:
    1. α-Keto acids
    2. α-Amino acids
    3. Fatty acids
    4. All of the above
(Ref. 1, p. 627)
  1. Loss of thiamin can be decreased by using:
    1. Unpolished rice
    2. Parboiled rice
    3. Whole wheat flour
    4. All of the above
(Ref. 6, p. 408)
  1. Daily requirement of thiamin is:
    1. 0.1 mg/1,000 Calories
    2. 0.5 mg/1,000 Calories
    3. 0.8 mg/1,000 Calories
    4. 1.0 mg/1,000 Calories
(Ref. 5, p. 207)
1 A
2 C
3 C
4 A
5 D
6 B
48
  1. Thiamin requirement is greater in:
    1. Fever
    2. Hyperthyroidism
    3. Alcoholism
    4. All of the above
(Ref. 5, p. 207)
  1. Wernicke's encephalopathy can occur in:
    1. Non-vegetarians
    2. Chronic alcoholics
    3. Pregnant women
    4. None of the above
(Ref. 1, p. 628)
  1. People consuming polished rice as their staple food are prone to:
    1. Beriberi
    2. Pellagra
    3. Scurvy
    4. None of the above
(Ref. 1, p. 628)
  1. Dry beriberi usually affects the:
    1. Cardiovascular system
    2. Alimentary system
    3. Central nervous system
    4. All of the above
(Ref. 6, p. 409)
  1. Concentration of pyruvic acid in blood is raised in:
    1. Diabetes mellitus
    2. Beriberi
    3. Pellagra
    4. Scurvy
(Ref. 3, p. 768)
  1. Thiamin diphosphate is required for the metabolism of all of the following except:
    1. Leucine
    2. Isoleucine
    3. Valine
    4. Lysine
(Ref. 1, p. 627)
  1. FMN and FAD can accept:
    1. Two hydrogen atoms
    2. Two electrons
    3. One hydrogen atom
    4. One electron
(Ref. 1, p.131)
  1. The following enzyme system is impaired in riboflavin deficiency:
    1. Succinate dehydrogenase
    2. Xanthine oxidase
    3. NADH dehydrogenase
    4. All of the above
(Ref. 1, p. 629)
7 D
8 B
9 A
10 C
11 B
12 D
13 A
14 D
49
  1. Daily requirement of riboflavin is:
    1. 0.5-1.0 mg
    2. 1.5-1.8 mg
    3. 2-5 mg
    4. 5-10 mg
(Ref. 5, p. 210)
  1. Riboflavin deficiency can cause:
    1. Peripheral neuritis
    2. Dementia
    3. Angular stomatitis
    4. Anaemia
(Ref. 1, p. 629)
  1. Pellagra occurs due to deficiency of:
    1. Thiamin
    2. Riboflavin
    3. Niacin
    4. Pyridoxine
(Ref. 1, p. 627)
  1. Nicotinic acid is also known as:
    1. Niacin
    2. Niacinamide
    3. Nicotinamide
    4. All of the above
(Ref. 1, p. 629)
  1. Synthesis of NAD from niacin requires:
    1. PRPP
    2. ATP
    3. Glutamine
    4. All of the above
(Ref. 1, p. 630)
  1. Niacin contains a:
    1. Sulphydryl group
    2. Carboxyl group
    3. Amide group
    4. All of the above
(Ref. 1, p. 630)
  1. Niacin deficiency can cause all of the following except:
    1. Digestive disorders
    2. Dermatitis
    3. Anaemia
    4. Dementia
(Ref. 1, p. 631)
  1. NADP is required as a coenzyme in:
    1. Glycolysis
    2. Citric acid cycle
    3. HMP shunt
    4. Gluconeogenesis
(Ref. 1, p. 631)
  1. NAD is required as a coenzyme for:
    1. Malate dehydrogenase
    2. Succinate dehydrogenase
    3. Glucose-6-phosphate dehydrogenase
    4. HMG CoA reductase
(Ref. 1, pp. 185, 220, 286)
15 B
16 C
17 C
18 A
19 D
20 B
21 C
22 C
23 A
50
  1. NAD is a coenzyme in all the following except:
    1. Citric acid cycle
    2. Glycolysis
    3. β-Oxidation of fatty acids
    4. HMP shunt
(Ref. 1, pp. 192, 241, 631)
  1. NAD contains:
    1. Adenine
    2. Deoxyribose
    3. Biotin
    4. None of the above
(Ref. 1, p. 630)
  1. Niacin can be synthesised in human beings from:
    1. Histidine
    2. Phenylalanine
    3. Tyrosine
    4. Tryptophan
(Ref. 1, p. 630)
  1. The following coenzyme is required for the synthesis of niacin:
    1. Thiamin diphosphate
    2. Flavin monophosphate
    3. Pyridoxal phosphate
    4. Tetrahydrofolate
(Ref. 1, p. 630)
  1. Excess of the following inhibits the endogenous synthesis of niacin:
    1. Lysine
    2. Leucine
    3. Isoleucine
    4. All of the above
(Ref. 1, p. 630)
  1. Daily requirement of niacin is:
    1. 5 mg
    2. 10 mg
    3. 20 mg
    4. 30 mg
(Ref. 5, p. 215)
  1. Niacin deficiency is common in people whose staple food is:
    1. Wheat
    2. Polished rice
    3. Maize and/or sorghum
    4. None of the above
(Ref. 1, p. 631)
  1. Niacin deficiency can occur in all the following conditions except:
    1. Deficient leucine intake
    2. Isoniazid administration
    3. Malignant carcinoid syndrome
    4. Hartnup disease
(Ref. 1, p. 631)
24 D
25 A
26 D
27 C
28 B
29 C
30 C
31 A
51
  1. Large doses of niacin:
    1. Increase serum cholesterol
    2. Decrease serum cholesterol
    3. Increase serum pyruvate
    4. Decrease serum pyruvate
(Ref. 1, p. 631)
  1. Niacin deficiency can occur in:
    1. Hartnup disease
    2. Phenylketonuria
    3. Alkaptonuria
    4. None of the above
(Ref. 1, p. 631)
  1. NAD+ and NADP+ accept:
    1. Two hydrogen atoms
    2. Two hydrogen atoms and an electron
    3. Two hydrogen atoms and two electrons
    4. One hydrogen atom and an electron
(Ref. 1, p. 631)
  1. Pantothenic acid contains an amino acid which is:
    1. Aspartic acid
    2. Glutamic acid
    3. β-Alanine
    4. β-Aminoisobutyric acid
(Ref. 1, p. 631)
  1. Pantothenic acid forms a coenzyme which is:
    1. PLP
    2. Cobamide
    3. Coenzyme A
    4. Coenzyme Q
(Ref. 1, p. 631)
  1. Sulphydryl group of coenzyme A is contributed by:
    1. β-Alanine
    2. β-Aminoisobutyric acid
    3. Methionine
    4. Thioethanolamine
(Ref. 1, p. 631)
  1. CoA participates in all the following except:
    1. Glycolysis
    2. Citric acid cycle
    3. Synthesis of fatty acids
    4. Synthesis of cholesterol
(Ref. 1, p. 631)
  1. Acyl carrier protein contains:
    1. Coenzyme A
    2. 4'-Phosphopantetheine
    3. 4'-Phosphopantethenyl cysteine
    4. Phosphopantothenic acid
(Ref. 1, p. 631)
32 B
33 A
34 D
35 C
36 C
37 D
38 A
39 B
52
  1. The following is required for the formation of coenzyme A:
    1. ATP
    2. GTP
    3. CTP
    4. None of the above
(Ref. 1, p. 631)
  1. Coenzyme A is required for oxidative decarboxylation of:
    1. Pyruvate
    2. Glutamate
    3. Isocitrate
    4. None of the above
(Ref. 1, pp. 184, 195, 316)
  1. Coenzyme A is required for catabolism of:
    1. Leucine
    2. Isoleucine
    3. Valine
    4. All of the above
(Ref. 1, p. 343)
  1. Daily requirement of pantothenic acid in adults is:
    1. 1-2 mg
    2. 5 mg
    3. 10 mg
    4. 20 mg
(Ref. 6, p. 417)
  1. Deficiency of pantothenic acid can cause:
    1. Microcytic anaemia
    2. Macrocytic anaemia
    3. Burning foot syndrome
    4. None of the above
(Ref. 1, p. 633)
  1. Pyridoxal phosphate forms a Schiff base with α-amino acids through a bond between:
    1. Hydroxyl group of PLP and carboxyl group of amino acid
    2. Hydroxyl group of PLP and α-amino group of amino acid
    3. Aldehyde group of PLP and carboxyl group of amino acid
    4. Aldehyde group of PLP and α-amino group of amino acid
(Ref. 1, p. 633)
  1. Pyridoxal phosphate is a coenzyme for:
    1. Glutamate oxaloacetate transaminase
    2. Glutamate pyruvate transaminase
    3. Tyrosine transaminase
    4. All of the above
(Ref. 1, p. 633)
40 A
41 A
42 D
43 C
44 C
45 D
46 D
53
  1. Pyridoxal phosphate is a coenzyme for:
    1. Arginase
    2. Asparaginase
    3. Glutaminase
    4. None of the above
(Ref. 1, pp. 320, 325)
  1. Pyridoxal phosphate is a coenzyme for all the following except:
    1. Kynureninase
    2. ALA synthetase
    3. DOPA decarboxylase
    4. Prolyl hydroxylase
(Ref. 1, pp. 311, 338, 356, 362)
  1. Pyridoxal phosphate acts as a coenzyme in:
    1. Glycogenesis
    2. Glycogenolysis
    3. Glycolysis
    4. None of the above
(Ref. 1, pp. 633-634)
  1. Pyridoxal phosphate is required as a coenzyme in the synthesis of:
    1. Haem
    2. Gamma amino butyric acid
    3. Niacin
    4. All of the above
(Ref. 1, pp. 356, 362, 631)
  1. Pyridoxine deficiency can be diagnosed by measuring urinary excretion of:
    1. Pyruvic acid
    2. Oxaloacetic acid
    3. Xanthurenic acid
    4. None of the above
(Ref. 1, p. 339)
  1. In pyridoxine deficiency, tryptophan is converted into:
    1. Nicotinic acid
    2. Acetoacetic acid
    3. Anthranilic acid
    4. Xanthurenic acid
(Ref. 1, p. 339)
  1. Pyridoxine deficiency can be diagnosed by measuring the urinary excretion of xanthurenic acid following a test dose of:
    1. Glycine
    2. Histidine
    3. Tryptophan
    4. Pyridoxine
(Ref. 1, p. 339)
47 D
48 D
49 B
50 D
51 C
520
53 C
54
  1. About 70 - 80 % of the total pyridoxine in the body is present in:
    1. Liver
    2. Muscles
    3. Adipose tissue
    4. Brain
(Ref. 1, p. 634)
  1. Pyridoxine deficiency can occur in tubercular patients taking:
    1. Isoniazid
    2. Para amino salicylate
    3. Streptomycin
    4. Thiacetazone
(Ref. 1, p. 634)
  1. Consumption of raw egg white can produce neurological abnormalities by blocking the absorption of:
    1. Pyridoxine
    2. Thiamin
    3. Biotin
    4. Lipoic acid
(Ref. 1, p. 635)
  1. Anti-egg white injury factor is:
    1. Pyridoxine
    2. Biotin
    3. Thiamin
    4. Lipoic acid
(Ref. 5, p. 223)
  1. The following protein in raw egg white forms a complex with biotin:
    1. Albumin
    2. Globulin
    3. Avidin
    4. Vitelline
(Ref. 1, p. 635)
  1. When eggs are cooked:
    1. Biotin is destroyed but avidin remains unaffected
    2. Avidin is inactivated but biotin remains unaffected
    3. Both avidin and biotin are inactivated
    4. Both avidin and biotin remain unaffected
(Ref. 6, p. 418)
  1. Biotin is a coenzyme for:
    1. Oxidases
    2. Decarboxylases
    3. Oxygenases
    4. Carboxylases
(Ref. 1, p. 634)
54 B
55 A
56 C
57 B
58 C
59 B
60 D
55
  1. Biotin is a coenzyme for:
    1. Pyruvate kinase
    2. Pyruvate dehydrogensase
    3. Pyruvate carboxylase
    4. PEP carboxykinase
(Ref. 1, p. 635)
  1. Biotin is a coenzyme for:
    1. Pyruvate carboxylase
    2. Acetyl CoA carboxylase
    3. Propionyl CoA carboxylase
    4. All of the above
(Ref. 1, p. 635)
  1. Lipoic acid can undergo reversible:
    1. Oxidation-reduction
    2. Sulphydration-desulphydration
    3. Both of the above
    4. Neither of the above
(Ref. 5, p. 219)
  1. Lipoic acid is a coenzyme for:
    1. Pyruvate dehydrogenase complex
    2. α-Ketoglutarate dehydrogenase complex
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 195)
  1. Oxidative decarboxylation of α-keto acids requires:
    1. Thiamin diphosphate, coenzyme A, lipoic acid and NAD
    2. Coenzyme A, lipoic acid, NAD and FAD
    3. Thiamin diphosphate, coenzyme A, NAD and FAD
    4. Thiamin diphosphate, coenzyme A, lipoic acid, NAD and FAD
(Ref. 1, p. 196)
  1. Chemically, lipoic acid is:
    1. Saturated fatty acid
    2. Unsaturated fatty acid
    3. Amino acid
    4. Sulphur-containing fatty acid
(Ref. 5, p. 219)
  1. Folic acid contains:
    1. Pteridine
    2. p-Amino benzoic acid
    3. Glutamic acid
    4. All of the above
(Ref. 1, p. 637)
61 C
62 D
63 A
64 C
65 D
66 D
67 D
56
  1. Conversion of folate into tetrahydrofolate requires:
    1. NADH
    2. NADPH
    3. FMNH2
    4. FADH2
(Ref. 1, p. 638)
  1. Aminopterin and amethopterin are:
    1. Folic acid antagonists
    2. Anticancer agents
    3. Competitive inhibitors of dihydrofolate reductase
    4. All of the above
(Ref. 5, pp. 230-232)
  1. Tetrahydrofolate can receive a one-carbon unit from:
    1. Serine
    2. Glycine
    3. Glutamate
    4. All of the above
(Ref. 1, p. 638)
  1. Tetrahydrofolate is required in the synthesis of all the following except:
    1. AMP
    2. GMP
    3. TMP
    4. UMP
(Ref. 1, pp. 387, 638)
  1. Deficiency of folic acid causes:
    1. Microcytic anaemia
    2. Normocytic anaemia
    3. Megaloblastic anaemia
    4. Polycythaemia
(Ref. 1, p. 638)
  1. Deficiency of folic acid can be diagnosed by measuring urinary formiminoglutamic acid following a test dose of:
    1. Tryptophan
    2. Methionine
    3. Histidine
    4. Glutamate
(Ref. 1, p. 638)
  1. Vitamin B12 may be present as:
    1. Methylcobalamin
    2. Adenosylcobalamin
    3. Hydroxycobalamin
    4. All of the above
(Ref. 1, p. 635)
  1. Vitamin B12 is required to form:
    1. Cobamides
    2. Transcobalamin I
    3. Transcobalamin II
    4. All of the above
(Ref. 1, pp. 76, 635)
68 B
69 D
70 A
71 D
72 C
73 C
74 D
75 A
57
  1. Methylcobalamin is required for formation of:
    1. Serine from glycine
    2. Glycine from serine
    3. Methionine from homocysteine
    4. All of the above
(Ref. 1, p. 637)
  1. Cobamide is a coenzyme for:
    1. Methylmalonyl CoA racemase
    2. Methylmalonyl CoA isomerase
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 210)
  1. Absorption of vitamin B12 requires the presence of:
    1. Pepsin
    2. Folic acid
    3. Extrinsic factor
    4. Intrinsic factor
(Ref. 1, p. 635)
  1. Intrinsic factor is synthesised in:
    1. Gastric mucosa
    2. Duodenal mucosa
    3. Jejunal mucosa
    4. Heal mucosa
(Ref. 1, p. 635)
  1. Intrinsic factor is chemically a:
    1. Protein
    2. Glycoprotein
    3. Mucopolysaccharide
    4. Peptide
(Ref. 1, p. 635)
  1. Chemically, extrinsic factor of Castle is a:
    1. Mucoprotein
    2. Glycoprotein
    3. Mucopolysaccharide
    4. Cyanocobalamin
(Ref. 5, p. 233)
  1. Vitamin B12 is:
    1. Not stored in the body
    2. Stored in bone marrow
    3. Stored in liver
    4. Stored in RE cells
(Ref. 1, p. 635)
  1. Vitamin B12 is stored in association with:
    1. Albumin
    2. Transcortin
    3. Transcobalamin I
    4. Transcobalamin II
(Ref. 1, p. 635)
76 C
77 B
78 D
79 A
80 B
81 D
82 C
83 C
58
  1. Vitamin B12 is transported in blood by:
    1. Albumin
    2. Transcortin
    3. Transcobalamin I
    4. Transcobalamin II
(Ref. 1, p. 635)
  1. Vitamin B12 is synthesised by:
    1. Bacteria only
    2. Plants only
    3. Animals only
    4. A and C
(Ref. 1, p. 635)
  1. Deficiency of vitamin B12 can occur because of:
    1. Decreased intake
    2. Gastrectomy
    3. Lack of intrinsic factor
    4. All of the above
(Ref. 1, p. 637)
  1. Deficiency of vitamin B12 can cause:
    1. Microcytic anaemia
    2. Normocytic anaemia
    3. Megaloblastic anaemia
    4. None of the above
(Ref. 1, p. 637)
  1. Deficiency of vitamin B12 can be diagnosed by:
    1. Carr-Price reaction
    2. Ames assay
    3. Watson-Schwartz test
    4. Schilling test
(Ref. 5, p. 238)
  1. Absence of intrinsic factor can cause:
    1. Megaloblastic anaemia
    2. Subacute combined degeneration
    3. Both of the above
    4. Neither of the above
(Ref. 5, p. 239)
  1. Gastrectomy leads to megaloblastic anaemia within a few:
    1. Days
    2. Weeks
    3. Months
    4. Years
(Ref. 6, p. 422)
  1. Human beings cannot synthesise ascorbic acid because they lack:
    1. Ascorbate dehydrogenase
    2. Xylulose reductase
    3. L-Gulonate dehydrogenase
    4. L-Gulonolactone oxidase
(Ref. 1, p. 640)
84 D
85 A
86 D
87 C
88 D
89 C
90 D
91 D
59
  1. Ascorbic acid is required to synthesise all of the following except:
    1. Collagen
    2. Bile acids
    3. Bile pigments
    4. Epinephrine
(Ref. 1, p. 640)
  1. Vitamin C enhances the intestinal absorption of:
    1. Potassium
    2. Iodine
    3. Iron
    4. None of the above
(Ref. 1, p. 641)
  1. Vitamin C activity is present in:
    1. D-Ascorbic acid
    2. D-Dehydroascorbic acid
    3. L-Ascorbic acid
    4. A and B
(Ref. 6, p. 426)
  1. Vitamin C is required for the hydroxylation of:
    1. Proline residues
    2. Lysine residues
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 311)
  1. Vitamin C is required for the synthesis of:
    1. Bile acids from cholesterol
    2. Bile salts from bile acids
    3. Vitamin D from cholesterol
    4. All of the above
(Ref. 1, p. 640)
  1. Deficiency of vitamin C causes:
    1. Beriberi
    2. Pellagra
    3. Pernicious anaemia
    4. Scurvy
(Ref. 1, p. 641)
  1. Deficiency of vitamin C causes all of the following except:
    1. Swollen gums
    2. Loose teeth
    3. Nerve degeneration
    4. Subcutaneous haemorrhages
(Ref. 1, p. 641)
92 C
93 C
94 C
95 C
96 A
97 D
98 C
60
  1. An early diagnosis of vitamin C deficiency can be made by:
    1. Measuring plasma ascorbic acid
    2. Measuring urinary ascorbic acid
    3. Ascorbic acid saturation test
    4. Any of the above
(Ref. 6, p. 427)
  1. Daily requirement of vitamin C in adults is about:
    1. 10 mg
    2. 25 mg
    3. 70 mg
    4. 100 mg
(Ref. 6, p. 427)
  1. The vitamin having the highest daily requirement amongst the following is:
    1. Thiamin
    2. Riboflavin
    3. Pyridoxine
    4. Ascorbic acid
(Ref. 1, p. 660)
  1. The vitamin having the lowest daily requirement amongst the following is:
    1. Niacin
    2. Pantothenic acid
    3. Folic acid
    4. Vitamin B12
(Ref. 1, p. 660)
  1. Anaemia can occur due to deficiency of all of the following except:
    1. Thiamin
    2. Pyridoxine
    3. Folic acid
    4. Vitamin B12
(Ref. 6, pp. 409, 415, 420, 423)
  1. A vitamin which can be synthesised by human beings is:
    1. Thiamin
    2. Niacin
    3. Folic acid
    4. Vitamin B12
(Ref. 1, pp. 628, 631, 635, 637)
  1. Laboratory diagnosis of vitamin B12 deficiency can be made by measuring the urinary excretion of:
    1. Xanthurenic acid
    2. Formiminoglutamic acid
    3. Methylmalonic acid
    4. Homogentisic acid
(Ref. 6, p. 423)
99 C
100 C
101 D
102 D
103 A
104 B
105 C

Fat-soluble Vitamins8

  1. Vitamin A activity is present in:
    1. Retinol
    2. Retinoic acid
    3. Retinal
    4. All of the above
(Ref. 1, p. 642)
  1. Vitamin A is stored in the body as:
    1. Free retinol
    2. Retinol ester
    3. Retinal
    4. Retinoic acid
(Ref. 1, p. 642)
  1. Precursor of vitamin A is:
    1. α -Carotene
    2. β -Carotene
    3. γ -Carotene
    4. All of the above
(Ref. 5, p. 186)
  1. Provitamin A is present in:
    1. Animals
    2. Vegetables
    3. Bacteria
    4. All of the above
(Ref. 1, p. 642)
  1. Two molecules of vitamin A can be formed from one molecule of:
    1. α -Carotene
    2. β -Carotene
    3. γ -Carotene
    4. All of the above
(Ref. 1, p. 642)
  1. Conversion of β-carotene into retinal requires the presence of:
    1. β-Carotene dioxygenase
    2. Bile salts
    3. Molecular oxygen
    4. All of the above
(Ref. 1, p. 642)
1 D
2 B
3 D
4 B
5 B
6 D
62
  1. Conversion of retinal into retinol requires the presence of:
    1. NADH
    2. NADPH
    3. FADH2
    4. Lipoic acid
(Ref. 1, p. 644)
  1. Retinal is converted into retinoic acid in the presence of:
    1. Retinal oxidase
    2. Retinal carboxylase
    3. Retinene reductase
    4. Spontaneously
(Ref. 5, p. 186)
  1. The following pair is interconvertible:
    1. Retinal and retinoic acid
    2. Retinal and retinol
    3. Retinol and retinoic acid
    4. All of the above
(Ref. 1, p. 643)
  1. Vitamin A absorbed in intestine is released into:
    1. Portal circulation
    2. Lacteals
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 642)
  1. Retinoic acid is transported in circulation by:
    1. Albumin
    2. Retinol binding protein
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 643)
  1. Vitamin A is stored in the body in:
    1. Liver
    2. Adipose tissue
    3. Reticuloendothelial cells
    4. All of the above
(Ref. 1, p. 643)
  1. Retinol-binding protein transports:
    1. Carotenes
    2. Retinol
    3. Retinoic acid
    4. All of the above
(Ref. 1, p. 643)
7 B
8 D
9 B
10 B
11 A
12 A
13 B
63
  1. Rhodopsin contains opsin and:
    1. 11-cis-Retinal
    2. 11-trans-Retinal
    3. All-cis-retinal
    4. All-trans-retinal
(Ref. 1, p. 643)
  1. When light falls on rod cells:
    1. All-cis-retinal is converted into all-trans-retinal
    2. 11-cis-Retinal is converted into 11-trans-retinal
    3. 11-trans-Retinal is converted into all-trans-retinal
    4. 11-cis-Retinal is converted into all-trans-retinal
(Ref. 1, p. 643)
  1. Retinol isomerase catalyses the interconversion of:
    1. All-trans-retinal and all-trans-retinol
    2. All-trans-retinol and 11-cis-retinol
    3. Both of the above
    4. Neither of the above
(Ref. 5, p. 188)
  1. Conversion of all-trans-retinal into all-trans-retinol requires:
    1. NAD
    2. NADH
    3. NADP
    4. NADPH
(Ref. 1, p. 644)
  1. Retinol isomerase is present in:
    1. Retina
    2. Liver
    3. Both of the above
    4. Neither of the above
(Ref. 5, p. 398)
  1. Anti-oxidant activity is present in:
    1. β-Carotene
    2. Retinol
    3. Retinoic acid
    4. All of the above
(Ref. 1, p. 644)
  1. All the functions of vitamin A can be performed by:
    1. Retinal
    2. Retinal and retinoic acid
    3. Retinal and retinol
    4. Retinol and retinoic acid
(Ref. 1, p. 643)
  1. One international unit of vitamin A is the activity present in:
    1. 0.3 μg of β-carotene
    2. 0.3μg of retinol
    3. 0.6μg of retinoic acid
    4. All of the above
(Ref. 5, p. 187)
14 A
15 D
16 B
17 D
18 B
19 A
20 C
21 B
64
  1. One retinol equivalent (RE) is the activity present in:
    1. Three μg of β-carotene
    2. One μg of β-carotene
    3. Three μg of retinol
    4. One μg of retinol
(Ref. 1, p. 660)
  1. Daily requirement of vitamin A in an adult man can be expressed as:
    1. 4001U
    2. 1000 IU
    3. 5,000 IU
    4. 110,000 IU
(Ref. 5, p. 187)
  1. In vitamin A deficiency, Bitot's spots appear on:
    1. Skin
    2. Retina
    3. Conjunctiva
    4. Cornea
(Ref. 5, p. 189)
  1. An early indication of vitamin A deficiency is:
    1. Xerophthalmia
    2. Keratomalacia
    3. Defective night vision
    4. Blindness
(Ref. 1, p. 643)
  1. Nyctalopia is:
    1. Drying of eyes
    2. Destruction of cornea
    3. Blindness
    4. Inability to see in dimlight
(Ref. 5, p. 189)
  1. When light falls on retina, the following change occurs in rod cells:
    1. Increase in cAMP concentration
    2. Decrease in cAMP concentration
    3. Increase in cGMP concentration
    4. Decrease in cGMP concentration
(Ref. 2, p. 336)
  1. Hyperpolarisation of rod cell membrane following exposure to light occurs due to:
    1. Opening of cation-specific channels
    2. Closure of cation-specific channels
    3. Opening of anion-specific channels
    4. Closure of anion-specific channels
(Ref. 2, p. 336)
22 D
23 C
24 D
25 C
26 D
27 D
28 B
65
  1. Signal is transmitted from receptor to effector in rod cells by:
    1. A Gs-protein
    2. A Gi-protein
    3. Adenylate cyclase
    4. cAMP phosphodiesterase
(Ref. 2, p. 336)
  1. A trans-membrane protein in rod cells is:
    1. Adenylate cyclase
    2. Transducin
    3. Rhodopsin
    4. Retinol isomerase
(Ref. 2, p. 334)
  1. One β-ionone ring is present in:
    1. Retinol
    2. α-Carotene
    3. Retinoic acid
    4. All of the above
(Ref. 5 pp. 185-186)
  1. Provitamins A include:
    1. Retinal
    2. Retinoic acid
    3. Carotenes
    4. All of the above
(Ref. 1, p. 642)
  1. Retinoic acid can:
    1. Act as a photoreceptor
    2. Support growth and differentiation
    3. Act as an anti-oxidant
    4. None of the above
(Ref. 1, p. 643)
  1. Hypervitaminosis A can occur when cells are exposed to high concentrations of:
    1. Unbound retinol
    2. Retinol bound to REP
    3. Retinol bound to CRBP
    4. All of the above
(Ref. 1, p. 643)
  1. Low density lipoprotein transports:
    1. Retinol
    2. Retinoic acid
    3. β-Carotene
    4. None of the above
(Ref. 1, p. 645)
  1. Prosthetic group in cone cell photoreceptors is:
    1. Iodine
    2. Opsin
    3. 11-cis-Retinal
    4. All-trans-retinal
(Ref. 6, p. 399)
29 A
30 C
31 D
32 C
32 B
34 A
35 C
36 C
66
  1. Retinoic acid is involved in the synthesis of:
    1. Rhodopsin
    2. Iodopsin
    3. Porphyrinopsin
    4. Glycoproteins
(Ref. 1, p. 643)
  1. Transducin is present in rod cells:
    1. On cell membrane
    2. Across cell membrane
    3. In cytosol
    4. In nucleus
(Ref. 2, pp. 334, 337)
  1. Transducin is a:
    1. Signal transducer
    2. Stimulatory G-protein
    3. Trimer
    4. All of the above
(Ref. 2, p. 336)
  1. Hyperpolarisation of rod cell membrane occurs due to:
    1. Increased cGMP concentration
    2. Increased cAMP concentration
    3. Decreased cGMP concentration
    4. Decreased cAMP concentration
(Ref. 2, pp. 336-337)
  1. Provitamin D3 is:
    1. Cholecalciferol
    2. Ergosterol
    3. 7-Dehydrocholesterol
    4. Ergocalciferol
(Ref. 1, p. 645)
  1. Ergocalciferol is:
    1. Provitamin D2
    2. Provitamin D3
    3. Vitamin D2
    4. Vitamin D3
(Ref. 1, p. 645)
  1. Ergosterol is found in:
    1. Animals
    2. Plants
    3. Bacteria
    4. All of the above
(Ref. 1, p. 645)
  1. A provitamin D synthesised in human beings is:
    1. Ergosterol
    2. 7-Dehydrocholesterol
    3. Cholecalciferol
    4. 25-Hydroxycholecalciferol
(Ref. 1, p. 645)
37 D
38 C
39 D
40 C
41 C
42 C
43 B
44 B
67
  1. Cholecalciferol is formed in:
    1. Intestinal mucosa
    2. Liver
    3. Skin
    4. Kidneys
(Ref. 1, p. 645)
  1. 25-Hydroxylation of vitamin D occurs in:
    1. Skin
    2. Liver
    3. Kidneys
    4. Intestinal mucosa
(Ref. 1, p. 645)
  1. 25-Hydroxycholecalciferol is hydroxylated at position 1 in:
    1. Kidneys
    2. Liver
    3. Skin
    4. Intestinal mucosa
(Ref. 1, p. 645)
  1. Tubular reabsorption of calcium is increased by:
    1. Cholecalciferol
    2. 25-Hydroxycholecalciferol
    3. Calcitriol.
    4. All of the above
(Ref. 5, p. 193)
  1. Immediate precursor of calcitriol is:
    1. 1-Hydroxycholecalciferol
    2. 25-Hydroxycholecalciferol
    3. 1, 25-Dihydroxycholecalciferol
    4. None of the above
(Ref. 1, p. 645)
  1. Calcitriol induces the synthesis of the following in the intestinal mucosa:
    1. Calcium-binding protein
    2. Ca++-Dependent ATPase
    3. Alkaline phosphatase
    4. All of the above
(Ref. 5, p. 192)
  1. Parathormone is required for the conversion of:
    1. Cholecalciferol into 1-hydroxycholecalciferol
    2. Cholecalciferol into 25-hydroxycholecalciferol
    3. 25-Hydroxycholecalciferol into calcitriol
    4. Cholesterol into 7-dehydrocholesterol
(Ref. 1, p. 573)
45 C
46 B
47 A
48 C
49 B
50 D
51 C
68
  1. Calcitriol inhibits the coversion of:
    1. Cholesterol into 7-dehydrocholesterol
    2. Cholecalciferol into 1-hydroxycholecalciferol
    3. Cholecalciferol into 25-hydroxycholecalciferol
    4. 25-Hroydroxycholecalciferol into 1, 25-dihydroxycholecalciferol
(Ref. 1, p. 5 73)
  1. Vitamin D activity of 10 μg of cholecalciferol is:
    1. 100 IU
    2. 2001U
    3. 250IU
    4. 4400 IU
(Ref. 1, p. 660)
  1. All of the following can occur in rickets except:
    1. Decrease in plasma calcium
    2. Decrease in plasma inorganic phosphorus
    3. Poor mineralisation of bones
    4. Soft tissue calcification
(Ref. 1, p. 573)
  1. Skeletal deformities can occur in:
    1. Rickets
    2. Osteomalacia
    3. Hypervitaminosis D
    4. All of the above
(Ref. 1, pp. 573-574)
  1. Calcification of soft tissues can occur in:
    1. Osteomalacia
    2. Rickets
    3. Hypervitaminosis D
    4. None of the above
(Ref. 5, pp. 193-194)
  1. Hypercalcaemia can occur in:
    1. Osteomalacia
    2. Rickets
    3. Hypoparathyroidism
    4. Hypervitaminosis D
(Ref. 5, p. 193)
  1. Plasma calcium and inorganic phosphorus are decreased in:
    1. Osteomalacia
    2. Hyperparathyroidism
    3. Hypervitaminosis D
    4. None of the above
(Ref. 1, pp. 571, 574, 658)
  1. The daily requirement of vitamin D in children is:
    1. 100 IU
    2. 200 IU
    3. 400 IU
    4. 600 IU
(Ref. 1, p. 660)
52 D
53 D
54 D
55 A
56 C
57 D
58 A
59 C
69
  1. A naturally occurring tocopherol of dietary significance is:
    1. Alpha - tocopherol
    2. Beta - tocopherol
    3. Gamma - tocopherol
    4. All of the above
(Ref. 1, p. 647)
  1. Requirement of vitamin E increases with the increasing intake of:
    1. Calories
    2. Proteins
    3. PUFA
    4. Cholesterol
(Ref. 1, p. 648)
  1. In human beings, vitamin E prevents:
    1. Sterility
    2. Hepatic necrosis
    3. Muscular dystrophy
    4. None of the above
(Ref. 6, pp. 404-405)
  1. Vitamin E protects:
    1. Polyunsaturated fatty acids against peroxidation
    2. Vitamin A and carotenes against oxidation
    3. Lung tissue against atmospheric pollutants
    4. All of the above
(Ref. 6, pp. 404-405)
  1. Vitamin K activity is present in:
    1. Phylloquinone
    2. Menaquinone
    3. Menadione
    4. All of the above
(Ref. 1, p. 650)
  1. Intestinal bacteria can synthesise:
    1. Phylloquinone
    2. Menaquinone
    3. Menadione
    4. None of the above
(Ref. 1, p. 651)
  1. A water-soluble form of vitamin K is:
    1. Phylloquinone
    2. Menaquinone
    3. Menadione
    4. None of the above
(Ref. 1, p. 649)
60 D
61 C
62 D
63 D
64 D
65 B
66 C
70
  1. Plasma level of the following is maintained by vitamin K:
    1. Prothrombin
    2. Proconvertin
    3. Christmas factor
    4. All of the above
(Ref. 1, p. 649)
  1. Prothrombin time is prolonged in:
    1. Vitamin K deficiency
    2. Liver damage
    3. Both of the above
    4. Neither of the above
(Ref. 5, p. 964)
  1. Menadione is converted in the body into:
    1. Menaquinone
    2. Phylloquinone
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 649)
  1. Hypervitaminosis can occur following prolonged intake of large doses of:
    1. Vitamins A and K
    2. Vitamins D and K
    3. Vitamins E and K
    4. Vitamins A and D
(Ref. 1, p. 642)
  1. Intestinal bacteria can synthesise:
    1. Vitamin A
    2. Vitamin D
    3. Vitamin E
    4. Vitamin K
(Ref. 1, pp. 642, 645, 647, 651)
  1. Hydroxylation of vitamin D at position 25 occurs in:
    1. Cytosol
    2. Mitochondria
    3. Endoplasmic reticulum
    4. Peroxisomes
(Ref. 1, p. 645)
  1. Hydroxylation of 25 - hydroxycholecalciferol at position 1 occurs in:
    1. Renal tubular cells
    2. Bones
    3. Placenta
    4. All of the above
(Ref. 1, p. 645)
  1. Hydroxylation of 25- hydroxycholecalciferol at position 1 occurs in:
    1. Mitochondria
    2. Endoplasmic reticulum
    3. Peroxisomes
    4. Lysosomes
(Ref. 1, p. 645)
67 D
68 C
69 A
70 D
71 D
72 C
73 D
74 A
71
  1. Vitamin E concentrates in:
    1. Cell membrane
    2. Mitochondrial membrane
    3. Membrane of endoplasmic reticulum
    4. All of the above
(Ref. 1, p. 647)
  1. Anti-oxidant action of vitamin E is particularly effective in:
    1. Erythrocyte membrane
    2. Membranes of respiratory tract
    3. Retina
    4. All of the above
(Ref. 1, p. 648)
  1. Vitamin E can be regenerated from its oxidised free radical form with the help of:
    1. Vitamin A
    2. Vitamin C
    3. Selenium
    4. All of the above
(Ref. 1, p. 650)
  1. Vitamin K is required to carboxylate:
    1. Glutamate residues of pre-prothrombin
    2. Aspartate residues of pre-prothrombin
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 649)
  1. Vitamin K:
    1. Increases transcription of the prothrombin gene
    2. Increases translation of the prothrombin mRNA
    3. Splits a peptide off pre-prothrombin
    4. None of the above
(Ref. 1, pp. 649-650)
  1. Dicoumarol:
    1. Is an inhibitor of vitamin K-dependent carboxylase
    2. Displaces Ca++ from prothrombin
    3. Is an inhibitor of 2,3-epoxide reductase
    4. Binds to γ-carboxyglutamate residues of prothrombin
(Ref. 1, p. 651)
75 D
76 D
77 B
78 A
79 D
80 C
72
  1. Fat-soluble vitamins have all the following common features except:
    1. They are isoprene derivatives
    2. Their absorption is linked to that of dietary fat
    3. They are transported in blood by some proteins
    4. They are prohormones
(Ref. 1, p. 642)
  1. As a source of vitamin A, weight for weight, β-carotene is:
    1. As effective as retinol
    2. Twice as effective as retinol
    3. Half as effective as retinol
    4. One-sixth as effective as retinol
(Ref. 1, p. 642)
  1. Retinol is transported from the intestine to liver by:
    1. Chylomicrons
    2. Retinol-binding protein
    3. HDL
    4. All of the above
(Ref. 1, p. 642)
  1. Daily requirement of vitamin A in adult men may be expressed as:
    1. 400 RE
    2. 600 RE
    3. 800 RE
    4. 1,000 RE
(Ref. 1, p. 660)
  1. 7-Dehydrocholesterol is the precursor of:
    1. Cholesterol
    2. Cholecalciferol
    3. Ergosterol
    4. Ergocalciferol
(Ref. 1, p. 645)
  1. The following can be formed from ergosterol:
    1. Cholesterol
    2. Cholecalciferol
    3. Ergocalciferol
    4. All of the above
(Ref. 1, p. 645)
  1. Conversion of 7-dehydrocholesterol into cholecalciferol occurs in:
    1. Intestinal mucosa
    2. Skin
    3. Liver
    4. Kidneys
(Ref. 1, p. 645)
81 D
82 D
83 A
84 D
85 B
86 C
87 B
73
  1. Vitamin D functions as a:
    1. Prohormone
    2. Modulator of hormone action
    3. Proenzyme
    4. Coenzyme
(Ref. 1, p. 645)
  1. Cholecalciferol and ergocalciferol differ in their:
    1. Vitamin D activity
    2. Ring portion
    3. Side chains
    4. All of the above
(Ref. 1, pp. 645, 646)
  1. A hormone formed from vitamin D is:
    1. Calcitonin
    2. Calcitriol
    3. 25-Hydroxycholecalciferol
    4. None of the above
(Ref. 1, p. 645)
  1. Vitamin D is transported in blood by:
    1. Albumin
    2. Vitamin D-binding protein
    3. Chylomicrons
    4. LDL
(Ref. 1, p. 645)
  1. The major vitamin D species in circulation is:
    1. Cholecalciferol
    2. 25-Hydroxycholecalciferol
    3. 1, 25 - Dihydroxycholecalciferol
    4. 24, 25 - Dihydroxycholecalciferol
(Ref. 1, p. 645)
  1. 24, 25 - Dihydroxycholecalciferol is:
    1. Formed in liver
    2. Formed from 1, 25 - dihydroxycholecalciferol by an isomerase
    3. Biologically inactive
    4. Formed when the calcitriol level is low
(Ref. 1, p. 647)
  1. The following can affect gene expression:
    1. Vitamins A and D
    2. Vitamins A and K
    3. Vitamins D and K
    4. Vitamins A and E
(Ref. 1, pp. 643, 647)
88 A
89 D
90 B
91 B
92 B
93 C
94 A
74
  1. 1-Hydroxylation of 25-hydroxycholecalciferol is increased by all the following except:
    1. Hypocalcaemia
    2. Hypophosphataemia
    3. Parathormone
    4. Calcitriol
(Ref. 1, p. 573)
  1. All the following statements about calcitriol receptor are true except:
    1. It is a member of the steroid receptor family
    2. It has a high-affinity ligand-binding domain
    3. It possesses zinc finger motif
    4. It is located in the cell membrane
(Ref. 1, p. 573)
  1. Vitamin E is transported from:
    1. The intestine to the extrahepatic tissues by chylomicrons
    2. The intestine to liver by chylomicron remnants
    3. Liver to extrahepatic tissues by VLDL
    4. All of the above
(Ref. 1, p. 647)
  1. 1-Hydroxylation of 25-hydroxycholecalciferol requires all the following except:
    1. NADH
    2. Molecular oxygen
    3. Cytochrome P-450
    4. Ferredoxin
(Ref. 1, p. 572)
  1. All the following statements about vitamin E are correct except:
    1. It acts as a chain-breaking anti-oxidant
    2. It is effective as an anti-oxidant at low oxygen concentrations
    3. It converts peroxyl free radical of PUFA into hydroperoxy-PUFA
    4. It reduces selenium requirement
(Ref. 1, pp. 647-649)
  1. As an anti-oxidant, vitamin E is effective against all of the following except:
    1. Singlet oxygen
    2. Superoxide free radicals
    3. Peroxyl free radicals
    4. Lipid peroxides
(Ref. 1, p. 649)
95 D
96 D
97 D
98 A
99 B
100 D

Porphyrins, Haemoglobin and Bilirubin9

  1. Porphyrin ring is present in all of the following except:
    1. Catalase
    2. Peroxidase
    3. Tryptophan pyrrolase
    4. Xanthine oxidase
(Ref. 1, pp. 131, 133, 360)
  1. Side chains of haem do not contain the following group:
    1. Acetate
    2. Propionate
    3. Methyl
    4. Vinyl
(Ref. 1, p. 361)
  1. The porphyrin present in haem is:
    1. Uroporphyrin
    2. Protoporphyrin I
    3. Coproporphyrin
    4. Protoporphyrin III
(Ref. 1, p. 361)
  1. An amino acid required for porphyrin synthesis is:
    1. Proline
    2. Glycine
    3. Serine
    4. Histidine
(Ref. 1, p. 359)
  1. An intermediate of the following pathway is required for the initial reaction of porphyrin synthesis:
    1. HMP shunt
    2. Glycolysis
    3. Krebs cycle
    4. Krebs-Henseleit cycle
(Ref. 1, p. 359)
1 D
2 A
3 D
4 B
5 C
76
  1. The following coenzyme is required for porphyrin synthesis:
    1. Coenzyme A
    2. Pyridoxal phosphate
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 362)
  1. The regulatory enzyme for haem synthesis is:
    1. ALA synthetase
    2. Haem synthetase
    3. Neither of the above
    4. Both of the above
(Ref. 1, p. 361)
  1. Regulation of haem synthesis occurs by:
    1. Covalent modification
    2. Repression-derepression
    3. Induction
    4. Allosteric regulation
(Ref. 1, p. 361)
  1. Two alpha and two beta chains are present in:
    1. Embryonic Hb
    2. Foetal Hb
    3. Hb A
    4. Hb A2
(Ref. 1, p. 66)
  1. Gamma polypeptide chains are present only in:
    1. Foetal Hb
    2. Hb A
    3. Embryonic Hb
    4. Hb S
(Ref. 1, p. 66)
  1. 2, 3-Biphosphoglycerate is attached to the following form of haemoglobin:
    1. T form
    2. R form
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 70)
  1. 2, 3-Biphosphoglycerate is released from haemoglobin when:
    1. Oxygen tension decreases
    2. Oxygen tension increases
    3. Glycolysis increases
    4. Glycolysis decreases
(Ref. 1, p. 70)
  1. Sigmoidal oxygen dissociation curve is a property of:
    1. Haemoglobin
    2. Carboxyhaemoglobin
    3. Myoglobin
    4. Methaemoglobin
(Ref. 1, pp. 66-67)
6 C
7 A
8 B
9 C
10 A
11 A
12 B
13 A
77
  1. Secondary and tertiary structures of myoglobin resemble those of:
    1. Alpha chain of Hb
    2. Beta chain of Hb
    3. Gamma chain of Hb
    4. Delta chain of Hb
(Ref. 1, p. 66)
  1. Hb S is formed by substitution of an amino acid at position 6 in:
    1. Alpha chain
    2. Beta chain
    3. Gamma chain
    4. Any chain
(Ref. 1, p. 71)
  1. In thalassaemia, an amino acid is substituted in:
    1. Alpha chain
    2. Beta chain
    3. Alpha and beta chains
    4. There is no substitution
(Ref. 1, p. 73)
  1. Haem synthetase is congenitally deficient in:
    1. Congenital erythropoietic porphyria
    2. Protoporphyria
    3. Hereditary coproporphyria
    4. Variegate porphyria
(Ref. 1, pp. 360, 366)
  1. During breakdown of haem, the methenyl bridge between the following two pyrrole rings is broken:
    1. I and II
    2. II and III
    3. III and IV
    4. IV and I
(Ref. 1, pp. 367-368)
  1. The number of sites for bilirubin binding on albumin is:
    1. One
    2. Two
    3. Three
    4. Four
(Ref. 1, p. 368)
  1. In 100 ml of blood having normal albumin concentration, the maximum quantity of bilirubin that can be bound to high affinity site of albumin is about:
    1. 1 mg
    2. 10 mg
    3. 15 mg
    4. 25 mg
(Ref. 1, p. 368)
  1. Pre-hepatic jaundice occurs because of:
    1. Increased haemolysis
    2. Liver damage
    3. Biliary obstruction
    4. None of the above
(Ref. 1, p. 373)
14 B
15 B
16 D
17 B
18 A
19 B
20 D
21 A
78
  1. Kernicterus can occur in:
    1. Retention hyperbilirubinaemia
    2. Regurgitation hyperbilirubinaemia
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 371)
  1. Unconjugated hyperbilirubinaemia can occur in:
    1. Neonatal jaundice
    2. Crigler-Najjar syndrome
    3. Gilbert's syndrome
    4. All of the above
(Ref. 1, p. 371)
  1. Bile pigments are not present in urine in:
    1. Haemolytic jaundice
    2. Hepatic jaundice
    3. Obstructive jaundice
    4. Rotor's syndrome
(Ref. 1, p. 372)
  1. Urinary urobilinogen is increased in:
    1. Haemolytic jaundice
    2. Hepatic jaundice
    3. Obstructive jaundice
    4. All of the above
(Ref. 1, p. 372)
  1. Urinary urobilinogen is absent in:
    1. Haemolytic jaundice
    2. Hepatic jaundice
    3. Obstructive jaundice
    4. None of the above
(Ref. 1, p. 372)
  1. Serum alkaline phosphatase is greatly increased in:
    1. Haemolytic jaundice
    2. Hepatic jaundice
    3. Obstructive jaundice
    4. None of the above
(Ref. 1, p. 83)
  1. The following is a harmless condition:
    1. Gilbert's syndrome
    2. Crigler-Najjar syndrome
    3. Rotor's syndrome
    4. Dubin-Johnson syndrome
(Ref. 1, p. 371)
22 A
23 D
24 A
25 A
26 C
27 C
28 A
79
  1. Bilirubin UDP-glucuronyl transferase is absent from liver in:
    1. Crigler-Najjar syndrome, type I
    2. Gilbert's syndrome
    3. Crigler-Najjar syndrome, type II
    4. Rotor's syndrome
(Ref. 1, p. 371)
  1. Conjugated bilirubin is raised in serum in:
    1. Crigler-Najjar syndrome
    2. Gilbert's syndrome
    3. Haemolytic anaemia
    4. Rotor's syndrome
(Ref. 1, p. 372)
  1. Unconjugated bilirubin in serum is raised in:
    1. Gilbert's syndrome
    2. Crigler-Najjar syndrome, type I
    3. Crigler-Najjar syndrome, type II
    4. All of the above
(Ref. 1, p. 371)
  1. Unconjugated bilirubin is soluble in:
    1. Water
    2. Alkalis
    3. Acids
    4. Methanol
(Ref. 1, p. 370)
  1. Conjugated bilirubin is soluble in:
    1. Water
    2. Methanol
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 370)
  1. Kernicterus can occur in:
    1. Crigler-Najjar syndrome, type I
    2. Crigler-Najjar syndrome, type II
    3. Rotor's syndrome
    4. None of the above
(Ref. 6, p. 363)
  1. Excretion of conjugated bilirubin from liver cells into biliary canaliculi is defective in:
    1. Gilbert's syndrome
    2. Crigler-Najjar syndrome
    3. Lucey-Driscoll syndrome
    4. Rotor's syndrome
(Ref. 1, pp. 371-372)
29 A
30 D
31 D
32 D
33 C
34 A
35 D
80
  1. Breakdown of one gm of haemoglobin produces:
    1. 20 mg of bilirubin
    2. 35 mg of bilirubin
    3. 50 mg of bilirubin
    4. 70 mg of bilirubin
(Ref. 1, p. 368)
  1. In a healthy adult, daily formation of bilirubin is:
    1. 50-100 mg
    2. 100-250 mg
    3. 250-350 mg
    4. 350-500 mg
(Ref. 1, p. 368)
  1. Daily urinary urobilinogen excretion in adult men is:
    1. 0-4 mg
    2. 5-8 mg
    3. 9-12 mg
    4. 13-20 mg
(Ref. 1, p. 372)
  1. Daily faecal urobilinogen excretion in healthy adults is:
    1. 0-40 mg
    2. 40-280 mg
    3. 280-500 mg
    4. 500-800 mg
(Ref. 1, p. 372)
  1. In obstructive jaundice, faecal urobilinogen is:
    1. Absent
    2. Decreased
    3. Increased
    4. Normal
(Ref. 1, p. 372)
  1. Haem proteins function in:
    1. Oxygen binding
    2. Oxygen transport
    3. Electron transport
    4. All of the above
(Ref. 1, p. 63)
  1. Oxidation of Fe++ destroys the biological activity of:
    1. Haemoglobin
    2. Cytochromes
    3. Both of the above
    4. Neither of the above
(Ref. 1, p.63)
  1. Haemoglobin can transport:
    1. Oxygen
    2. Carbon dioxide
    3. Protons
    4. All of the above
(Ref. 1, p. 66)
  1. Synthesis of β chains of haemoglobin occurs in the following period of pregnancy:
    1. First trimester
    2. Second trimester
    3. Third trimester
    4. All of the above
(Ref. 1, p.67)
36 B
37 C
38 A
39 B
40 A
41 D
42 A
43 D
44 C
81
  1. 2, 3 - Biphosphoglycerate binds to:
    1. Alpha chains of Hb
    2. Beta chains of Hb
    3. Haem group of Hb
    4. All of the above
(Ref. 1, p. 70)
  1. Foetal haemoglobin:
    1. Does not bind 2,3 - biphosphoglycerate
    2. Binds 2,3 - biphosphoglycerate less strongly than adult haemoglobin
    3. Binds 2,3 - biphosphoglycerate more strongly than adult haemoglobin
    4. Binds 2,3 - biphosphoglycerate equally strongly as adult haemoglobin
(Ref. 1, p.70)
  1. All the following statements about haemoglobin M are correct except:
    1. It is formed by replacement of the distal histidine (E7) residue by tyrosine
    2. Phenolate group of tyrosine forms a tight ionic complex with iron
    3. Iron is stabilised in the ferric state
    4. It can not combine with oxygen
(Ref. 1, p.70)
  1. All the following statements about haemoglobin S are correct except:
    1. It is formed by replacement of valine residue at position 6 in the β chain by glutamate
    2. It has altered surface properties
    3. It is capable of combining with oxygen
    4. Deoxygenated Hb S gets polymerised into helical fibers
(Ref. 1, p.71)
  1. Glycosylated haemoglobin:
    1. Is not present in normal persons
    2. Is formed by enzymatic glycosylation of haemoglobin
    3. Is formed due to a defective glycosyl transferase
    4. Has glucose residues attached to amino groups of haemoglobin
(Ref. 1, p. 72)
45 B
46 B
47 A
48 A
49 D
82
  1. All the following statements about glycosylated haemoglobin are correct except:
    1. It is formed by non-enzymatic glycosylation of haemoglobin
    2. It has glucose residues attached to serine, threonine or tyrosine residues of haemoglobin.
    3. It is normally about 5% of the total haemoglobin
    4. It is elevated when control of diabetes mellitus is poor
(Ref. 1, p. 72)
50 B

Pyruvate Metabolism and Citric Acid Cycle10

  1. Pyruvate carboxylase acts in the presence of:
    1. Biotin
    2. Mg++
    3. ATP
    4. All of the above
(Ref. 1, p. 636)
  1. Pyruvate carboxylase is allosterically inhibited by:
    1. Pyruvate
    2. ATP
    3. Oxaloacetate
    4. ADP
(Ref. 1, p. 212)
  1. Allosteric activator of pyruvate carboxylase is:
    1. Acetyl CoA
    2. ATP
    3. Oxaloacetate
    4. Pyruvate
(Ref. 1, p. 212)
  1. Oxaloacetate can be formed from:
    1. Pyruvate
    2. Aspartate
    3. Both of the above
    4. Neither of the above
(Ref. 1, pp. 209, 325)
  1. Acetyl CoA can be formed from:
    1. Pyruvate
    2. Fatty acids
    3. Ketone bodies
    4. All of the above
(Ref. 1, pp. 209, 243)
  1. Pyruvate is converted into acetyl CoA by:
    1. Decarboxylation
    2. Dehydrogenation
    3. Oxidative decarboxylation
    4. Oxidative deamination
(Ref. 1, p. 195)
1 D
2 D
3 A
4 C
5 D
6 C
84
  1. Conversion of pyruvate into acetyl CoA is catalysed by:
    1. Pyruvate dehydrogenase
    2. Dihydrolipoyl acetyl transferase
    3. Dihydrolipoyl dehydrogenase
    4. All the three acting in concert
(Ref. 1, p. 195)
  1. Coenzyme required for oxidative decarboxylation of pyruvate is:
    1. Thiamin pyrophosphate
    2. NAD
    3. FAD
    4. All of the above
(Ref. 1, p. 196)
  1. All of the following are required for oxidative decarboxylation of pyruvate except:
    1. Coenzyme A
    2. Lipoic acid
    3. Pyridoxal phosphate
    4. FAD
(Ref. 1, p. 196)
  1. Pyruvate dehydrogenase complex is located in:
    1. Cytosol
    2. Lysosomes
    3. Mitochondria
    4. Endoplasmic reticulum
(Ref. 1, p. 195)
  1. A flavoprotein in pyruvate dehydrogenase complex is:
    1. Pyruvate dehydrogenase
    2. Dihydrolipoyl acetyl transferase
    3. Dihydrolipoyl dehydrogenase
    4. None of the above
(Ref. 1, p. 195)
  1. The ratio of pyruvate dehydrogenase, dihydrolipoyl acetyl transferase and dihydrolipoyl dehydrogenase subunits in pyruvate dehydrogenase complex is:
    1. 1:1:1
    2. 1:1:2
    3. 2:1:1
    4. 2:2:1
(Ref. 2, p. 515)
  1. The total number of polypeptide chains in pyruvate dehydrogenase complex is:
    1. 60
    2. 30
    3. 12
    4. 6
(Ref. 2, p. 515)
7 D
8 D
9 C
10 C
11 C
12 D
13 A
85
  1. Pyruvate dehydrogenase complex is regulated by:
    1. Covalent modification
    2. Allosteric regulation
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 197)
  1. An allosteric inhibitor of pyruvate dehydrogenase is:
    1. Acetyl CoA
    2. ATP
    3. NAD
    4. Aspartate
(Ref. 1, p. 197)
  1. Pyruvate dehydrogenase kinase is inhibited by:
    1. Acetyl CoA
    2. ATP
    3. NADH
    4. Pyruvate
(Ref. 1, p. 197)
  1. Pyruvate dehydrogenase kinase is activated by:
    1. Acetyl CoA
    2. ATP
    3. NADH
    4. All of the above
(Ref. 1, p. 197)
  1. All the following are tricarboxylic acids except:
    1. Oxaloacetate
    2. cis-Aconitate
    3. Oxalosuccinate
    4. Citrate
(Ref. 1, p. 185)
  1. Enzymes of citric acid cycle are present in:
    1. Cytosol
    2. Mitochondria
    3. Lysosomes
    4. All of the above
(Ref. 1, p. 184)
  1. In adipose tissue, pyruvate dehydrogenase phosphatase is activated by:
    1. Ca++
    2. Mg++
    3. Insulin
    4. None of the above
(Ref. 1, p. 197)
  1. In citric acid cycle, NAD is reduced in:
    1. One reaction
    2. Two reactions
    3. Three reactions
    4. Four reactions
(Ref. 1, p. 186)
  1. Among citric acid cycle enzymes, a flavoprotein is:
    1. Malate dehydrogenase
    2. Fumarase
    3. Succinate dehydrogenase
    4. Isocitrate dehydrogenase
(Ref. 1, p. 186)
14 C
15 A
16 D
17 D
18 A
19 B
20 C
21 C
22 C
86
  1. Malate dehydrogenase acts on:
    1. D-Malate
    2. L-Malate
    3. DL-Malate
    4. All of the above
(Ref. 1, p. 186)
  1. In citric acid cycle, GDP is phosphorylated by:
    1. Succinate dehydrogenase
    2. Aconitase
    3. Succinate thiokinase (Succinyl CoA synthetase)
    4. Fumarase
(Ref. 2, p. 513)
  1. Fluoroacetate is an inhibitor of:
    1. Citrate synthetase
    2. Aconitase
    3. Fumarase
    4. Succinate dehydrogenase
(Ref. 1, p. 185)
  1. Malonate is an inhibitor of:
    1. Malate dehydrogenase
    2. α-Ketoglutarate dehydrogenase
    3. Succinate dehydrogenase
    4. Isocitrate dehydrogenase
(Ref. 1, p. 186)
  1. When one molecule of acetyl CoA is oxidised in citric acid cycle, the net energy yield is:
    1. 2 ATP equivalents
    2. 8 ATP equivalents
    3. 12 ATP equivalents
    4. 15 ATP equivalents
(Ref. 1, p. 186)
  1. Citrate synthetase is allosterically inhibited by:
    1. ATP
    2. Isocitrate
    3. NADH
    4. Citrate
(Ref. 1, p. 189)
  1. Isocitrate dehydrogenase is allosterically activated by:
    1. Citrate
    2. α-Ketoglutarate
    3. ADP
    4. NAD
(Ref. 1, p.189)
  1. α-Ketoglutarate dehydrogenase is allosterically inhibited by:
    1. NADH
    2. Succinyl CoA
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 189)
23 B
24 C
24 B
26 C
27 C
28 A
29 C
30 C
87
  1. All of the following are allosteric enzymes except:
    1. Citrate synthetase
    2. α-Ketoglutarate dehydrogenase
    3. Succinate thiokinase
    4. Succinate dehydrogenase
(Ref. 1, p. 189)
  1. In citric acid cycle, FAD is reduced by:
    1. Isocitrate dehydrogenase
    2. α-Ketoglutarate dehydrogenase
    3. Succinate dehydrogenase
    4. Malate dehydrogenase
(Ref. 1, p. 185)
  1. All the following are dicarboxylic acids except:
    1. cis-Aconitate
    2. Succinate
    3. Fumarate
    4. Malate
(Ref. 1, p. 185)
  1. All the following are intermediates of citric acid cycle except:
    1. Oxalosuccinate
    2. Oxaloacetate
    3. Pyruvate
    4. Fumarate
(Ref. 1, p. 185)
  1. All the following intermediates of citric acid cycle can be formed from amino acids except:
    1. α-Ketoglutarate
    2. Fumarate
    3. Malate
    4. Oxaloacetate
(Ref. 1, p. 187)
  1. Intermediates of citric acid cycle which can form amino acids are:
    1. Oxaloacetate and isocitrate
    2. Oxaloacetate and α-ketoglutarate
    3. α-Ketoglutarate and succinate
    4. α-Ketoglutarate and fumarate
(Ref 1, p.187)
  1. Arsenite inhibits:
    1. Isocitrate dehydrogenase
    2. α-Ketoglutarate dehydrogenase
    3. Succinate thiokinase
    4. Succinate dehydrogenase
(Ref. 1, p.185)
31 C
32 C
33 A
34 C
35 C
36 B
37 B
88
  1. The reaction catalysed by the following enzyme is functionally irreversible:
    1. Citrate synthetase
    2. Aconitase
    3. Isocitrate dehydrogenase
    4. Succinate thiokinase
(Ref. 1, p. 185)
  1. Two functionally irreversible reactions in citric acid cycle are catalysed by:
    1. Citrate synthetase and α-ketoglutarate dehydrogenase
    2. Aconitase and isocitrate dehydrogenase
    3. Succinate thiokinase and succinate dehydrogenase
    4. Fumarase and malate dehydrogenase
(Ref. 1, p.185)
  1. NAD is reduced in reactions catalysed by all of the following enzymes of citric acid cycle except:
    1. Isocitrate dehydrogenase
    2. α-Ketoglutarate dehydrogenase
    3. Succinate dehydrogenase
    4. Malate dehydrogenase
(Ref. 1, p. 185)
  1. Two decarboxylation reactions in citric acid cycle are catalysed by:
    1. Aconitase and isocitrate dehydrogenase
    2. Isocitrate dehydrogenase and α-ketoglutarate dehydrogenase
    3. Oxalosuccinate decarboxylase and fumarase
    4. α-Ketoglutarate dehydrogenase and fumarase
(Ref. 1, p.185)
  1. The correct sequence of tricarboxylic acid intermediates in citric acid cycle is:
    1. Citrate, isocitrate and cis-aconitate
    2. Isocitrate, citrate and cis-aconitate
    3. Citrate, cis-aconitate and isocitrate
    4. cis-aconitate, citrate and isocitrate
(Ref. 1, p.185)
38 A
39 A
40 C
41 B
42 C
89
  1. The correct sequence of dicarboxylic acid intermediates in citric acid cycle is:
    1. Succinate, fumarate, malate and oxaloacetate
    2. Fumarate, succinate, malate and oxaloacetate
    3. Malate, fumarate, succinate and oxaloacetate
    4. Succinate, malate, fumarate and oxaloacetate
(Ref. 1, p.185)
  1. A citric acid cycle intermediate which can provide acetyl CoA for fatty acid synthesis is:
    1. Citrate
    2. Isocitrate
    3. α-Ketoglutarate
    4. Oxaloacetate
(Ref. 1, p.188)
  1. In muscles, calcium ions activate:
    1. Citrate synthetase
    2. Isocitrate dehydrogenase
    3. α-Ketoglutarate dehydrogenase
    4. All of the above
(Ref. 1, p.189)
  1. Coenzyme A is released in the reaction catalysed by:
    1. Citrate synthetase
    2. α-Ketoglutarate dehydrogenase
    3. ATP-citrate lyase
    4. All of the above
(Ref. 1, pp. 185, 188, 189)
  1. An intermediate of citric acid cycle which can be directly converted into phosphoenolpyruvate is:
    1. Citrate
    2. Isocitrate
    3. Succinate
    4. Oxaloacetate
(Ref. 1, p.187)
  1. The reactions catalysed by all of the following are physiologically reversible except:
    1. Aconitase
    2. α-Ketoglutarate dehydrogenase
    3. Succinate dehydrogenase
    4. Malate dehydrogenase
(Ref. 1, p.185)
43 A
44 A
45 D
46 A
47 D
48 B
90
  1. Rate of citric acid cycle reactions may be influenced by all of the following except:
    1. ATP
    2. NADH
    3. FADH2
    4. Ca++
(Ref. 1, p.189)
  1. Long-chain fatty acyl CoA inhibits:
    1. Isocitrate dehydrogenase
    2. α-Ketoglutarate dehydrogenase
    3. Citrate synthetase
    4. Malate dehydrogenase
(Ref. 1, p.185)
49 C
50 C

Metabolism of Carbohydrates11

  1. Glycolytic pathway is located in:
    1. Mitochondria
    2. Cytosol
    3. Microsomes
    4. Nucleus
(Ref. 1, p. 191)
  1. End product of aerobic glycolysis is:
    1. Acetyl CoA
    2. Lactate
    3. Pyruvate
    4. CO2 and H2O
(Ref. 1, p. 194)
  1. During fasting, glucose is phosphorylated mainly by:
    1. Hexokinase
    2. Glucokinase
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 191)
  1. The following is an inducible enzyme:
    1. Glucokinase
    2. Hexokinase
    3. Phosphohexose isomerase
    4. Aldolase
(Ref. 1, p. 191)
  1. Glucokinase is found in:
    1. Muscles
    2. Brain
    3. Liver
    4. All of the above
(Ref. 1, p. 191)
  1. Fluoride ions inhibit:
    1. Aldolase
    2. Enolase
    3. Glucokinase
    4. Pyruvate kinase
(Ref. 1, p. 192)
1 B
2 C
3 A
4 A
5 C
6 B
92
  1. During aerobic glycolysis, energy yield from each molecule of glucose is:
    1. 2 ATP equivalents
    2. 8 ATP equivalents
    3. 10 ATP equivalents
    4. 30 ATP equivalents
(Ref. 1, p. 198)
  1. In anaerobic glycolysis, energy yield from each molecule of glucose is:
    1. 2 ATP equivalents
    2. 8 ATP equivalents
    3. 30 ATP equivalents
    4. 38 ATP equivalents
(Ref. 1, p. 198)
  1. The reaction catalysed by the following enzyme is freely reversible:
    1. Hexokinase
    2. Phosphohexose isomerase
    3. Pyruvate kinase
    4. Phosphofructokinase
(Ref. 1, p. 192)
  1. The following is an allosteric enzyme:
    1. Phosphohexose isomerase
    2. Phosphotriose isomerase
    3. Lactate dehydrogenase
    4. Phosphofructokinase
(Ref. 1, p. 212)
  1. The following is not an allosteric enzyme:
    1. Glucokinase
    2. Hexokinase
    3. Phosphofructokinase
    4. Pyruvate kinase
(Ref. 1, pp. 191, 212)
  1. Glycolysis is always anaerobic in:
    1. Liver
    2. Brain
    3. Kidneys
    4. Erythrocytes
(Ref. 1, p. 195)
  1. Phosphofructokinase is allosterically inhibited by:
    1. Fructose-1, 6-biphosphate
    2. Lactate
    3. Pyruvate
    4. Citrate
(Ref. 1, p. 212)
7 B
8 A
9 B
10 D
11 A
12 D
13 D
93
  1. Glucose-6-phosphate is an allosteric inhibitor of:
    1. Glucokinase
    2. Hexokinase
    3. Phosphohexose isomerase
    4. None of the above
(Ref. 1, p. 212)
  1. The following is an allosteric enzyme:
    1. Hexokinase
    2. Phosphofructokinase
    3. Pyruvate kinase
    4. All of the above
(Ref. 1, p. 212)
  1. ATP is a co-substrate as well as an allosteric inhibitor of:
    1. Phosphofructokinase
    2. Hexokinase
    3. Glucokinase
    4. None of the above
Ref 1, pp.212-213)
  1. Pyruvate kinase is inhibited by:
    1. Enol pyruvate
    2. Lactate
    3. Citrate
    4. Alanine
(Ref. 1, p. 212)
  1. Complete oxidation of one molecule of glucose into CO2 and H2O yields:
    1. 8 ATP equivalents
    2. 15 ATP equivalents
    3. 30 ATP equivalents
    4. 38 ATP equivalents
(Ref. 1, p. 198)
  1. A substrate-linked phosphorylation in glycolysis is catalysed by:
    1. Hexokinase
    2. Phosphofructokinase
    3. Phosphoglycerate kinase
    4. Pyruvate kinase
(Ref. 1, p. 194)
  1. A unique by-product of glycolysis in erythrocytes is:
    1. Lactate
    2. 1, 3-Biphosphoglycerate
    3. 2, 3-Biphosphoglycerate
    4. All of the above
(Ref. 1. p. 195)
14 B
15 D
16 A
16 D
18 D
19 C
20 C
94
  1. When glycolysis occurs in erythrocytes via 2, 3-biphosphoglycerate, the net energy yield from one molecule of glucose is:
    1. Zero
    2. 2 ATP equivalents
    3. 4 ATP equivalents
    4. 8 ATP equivalents
(Ref. 1. p. 195)
  1. Inorganic phosphate is incorporated in the substrate by:
    1. Glyceraldehyde-3-phosphate dehydrogenase
    2. Phosphoglycerate kinase
    3. Pyruvate kinase
    4. Enolase
(Ref. 1, p.193)
  1. Biphosphoglycerate mutase is present in:
    1. Liver
    2. Muscles
    3. Brain
    4. Erythrocytes
(Ref. 1, p.195)
  1. Glycerol can enter glycolytic pathway via:
    1. Dihydroxyacetone phosphate
    2. 1, 3-Biphosphoglycerate
    3. 3-Phosphoglycerate
    4. 2-Phosphoglycerate
(Ref. 1, p. 210)
  1. Enzymes of hexose monophosphate shunt are present in:
    1. Mitochondria
    2. Cytosol
    3. Lysosomes
    4. Microsomes
(Ref. 1, p. 219)
  1. HMP shunt is present in:
    1. Erythrocytes
    2. Liver
    3. Testes
    4. All of the above
(Ref. 1, p. 221)
  1. In HMP shunt, reducing equivalents are accepted by:
    1. NAB
    2. NADP
    3. FMN
    4. FAD
(Ref. 1, p. 219)
  1. HMP shunt produces:
    1. ATP
    2. NADH
    3. NADPH
    4. All of the above
(Ref. 1, p. 221)
21 A
22 A
23 D
24 A
25 B
26 D
27 B
28 C
95
  1. Glucose-6-phosphate dehydrogenase is induced by:
    1. 6-Phosphogluconolactone
    2. Glucose-6-phosphate
    3. Ribose-5-phosphate
    4. Insulin
(Ref. 1, p. 221)
  1. The decarboxylation reaction in HMP shunt is catalysed by:
    1. Gluconolactone hydrolase
    2. 6-Phosphogluconate decarboxylase
    3. 6-Phosphogluconate dehydrogenase
    4. Transaldolase
(Ref. 1, p. 220)
  1. The first pentose formed in HMP shunt is:
    1. Ribose-5-phosphate
    2. Ribulose-5-phosphate
    3. Xylose-5-phosphate
    4. Xylulose-5-phosphate
(Ref. 1, p. 220)
  1. The coenzyme for transketolase is:
    1. NADP
    2. NAD
    3. Thiamin pyrophosphate
    4. No coenzyme is required
(Ref. 1, p. 221)
  1. The number of NADP molecules reduced per molecule of glucose-6-phosphate converted into ribulose-5-phosphate is:
    1. One
    2. Two
    3. Six
    4. Twelve
(Ref. 1, p. 220)
  1. The regulatory enzyme in HMP shunt is:
    1. Glucose-6-phosphate dehydrogenase
    2. 6-Phosphogluconate dehydrogenase
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 221)
  1. The rate of HMP shunt reactions is:
    1. Increased by insulin
    2. Increased in diabetes mellitus
    3. Increased by glucagon
    4. Increased in starvation
(Ref. 1, p. 212)
29 D
30 C
31 B
32 C
33 B
34 C
35 A
96
  1. The coenzymes required in HMP shunt are formed from:
    1. Thiamin and pyridoxine
    2. Niacin and pyridoxine
    3. Thiamin and niacin
    4. Niacin and folic acid
(Ref. 1, pp. 220-221)
  1. Glycogenesis requires:
    1. GTP
    2. CTP
    3. UTP
    4. None of the above
(Ref. 1, p. 200)
  1. Substrates for glycogen synthetase are glycogen primer and:
    1. Glucose
    2. UDP-Glucose
    3. Glucose-1-phosphate
    4. Glucose-6-phosphate
(Ref. 1, p. 200)
  1. Glycogen synthetase catalyses the formation of:
    1. α-1, 4-Glycosidic bonds
    2. α-1, 6-Glycosidic bonds
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 200)
  1. The energy spent for addition of each glucose unit to the glycogen primer is:
    1. One ATP equivalent
    2. Two ATP equivalents
    3. Three ATP equivalents
    4. Four ATP equivalents
(Ref. 1, p. 200)
  1. Glycogenesis is increased by:
    1. Glucagon
    2. Insulin
    3. Epinephrine
    4. cAMP
(Ref. 1, p. 212)
  1. Glycogen synthetase is activated by:
    1. Phosphorylation
    2. Adenylation
    3. Dephosphorylation
    4. Deadenylation
(Ref. 1, p. 204)
  1. Hepatic glycogenolysis is increased by:
    1. Insulin
    2. Glucagon
    3. Epinephrine
    4. Glucocorticoids
(Ref. 1, p. 205)
36 C
37 C
38 B
39 A
40 B
41 B
42 C
43 B
97
  1. Glycogen phosphorylase hydrolyses:
    1. α-1, 6-Glycosidic bonds
    2. α-1, 4-Glycosidic bonds
    3. β-1, 4-Glycosidic bonds
    4. All of the above
(Ref. 1, p. 201)
  1. Glycogen phosphorylase liberates the following from glycogen:
    1. Glucose
    2. Glucose-6-phosphate
    3. Glucose-1-phosphate
    4. Maltose
(Ref. 1, p. 201)
  1. After the action of phosphorylase, glycogen is converted into:
    1. Amylopectin
    2. Limit dextrin
    3. Amylose
    4. Maltose
(Ref. 1, p. 206)
  1. α-1, 6-Glycosidic bonds of glycogen are hydrolysed by:
    1. Amylo-1, 4 → 1, 6-transglucosidase
    2. Debranching enzyme
    3. Isomaltase
    4. Amylase
(Ref. 1, p. 202)
  1. Amylo-1, 6-glucosidase liberates the following from glycogen:
    1. Glucose-1-phosphate
    2. Glucose-6-phosphate
    3. Maltose
    4. Glucose
(Ref. 1, pp. 200-201)
  1. Glucose-1-phosphate liberated from glycogen cannot be converted into free glucose in:
    1. Liver
    2. Kidneys
    3. Muscles
    4. Brain
(Ref. 1, p. 201)
  1. During glycogenolysis, glucose-1-phosphate and glucose are liberated in the ratio of approximately:
    1. 30:1
    2. 24:1
    3. 10:1
    4. 1:1
(Ref. 2, p. 588)
  1. A coenzyme present in muscle phosphorylase is:
    1. NAD
    2. Pyridoxal phosphate
    3. Thiamin pyrophosphate
    4. Coenzyme A
(Ref. 1, p. 202)
44 B
45 C
46 B
47 B
48 D
49 C
50 C
51 B
98
  1. Generally, glycogenolysis in muscles is immediately followed by:
    1. Glycolysis
    2. Gluconeogenesis
    3. HMP shunt
    4. Lipogenesis
(Ref. 1, p. 199)
  1. If glucose-1-phosphate formed by glycogenolysis in muscles is oxidised to CO2 and H2O, the energy yield will be:
    1. 38 ATP equivalents
    2. 8 ATP equivalents
    3. 39 ATP equivalents
    4. 2 ATP equivalents
(Ref. 3, pp. 415-416, 497-498)
  1. If glucose-1-phosphate formed by glycogenolysis in muscles is catabolised to lactate, the energy yield will be:
    1. 2 ATP equivalents
    2. 3 ATP equivalents
    3. 4 ATP equivalents
    4. 8 ATP equivalents
(Ref. 1, p. 198)
  1. If glucose-1-phosphate formed by glycogenolysis in muscles is oxidised to pyruvate, the energy yield will be:
    1. 2 ATP equivalents
    2. 3 ATP equivalents
    3. 8 ATP equivalents
    4. 9 ATP equivalents
(Ref. 1, p. 198)
  1. A molecule of phosphorylase kinase is made up of:
    1. 4 subunits
    2. 8 subunits
    3. 12 subunits
    4. 16 subunits
(Ref. 1, p. 202)
  1. In the inactive form of phosphorylase kinase:
    1. α-and β-subunits are phosphorylated
    2. α-and β-subunits are not phosphorylated
    3. γ-and δ-subunits are phosphorylated
    4. Calcium ions are bound to β-subunits
(Ref. 1, p. 204)
52 A
53 C
54 B
55 D
56 D
57 B
99
  1. The following subunits of phosphorylase kinase bind calcium ions:
    1. α-subunits
    2. β-subunits
    3. γ-subunits
    4. δ-subunits
(Ref. 1, p. 204)
  1. The catalytic activity of phosphorylase kinase is present in:
    1. α-subunits
    2. β-subunits
    3. γ-subunits
    4. δ-subunits
(Ref. 1, p. 204)
  1. The calcium-bound δ-subunits of phosphorylase kinase are identical in structure to:
    1. Actin
    2. Myosin
    3. Calmodulin
    4. Prothrombin
(Ref. 1, p. 204)
  1. cAMP-dependent protein kinase phosphorylates:
    1. Glycogen synthetase a
    2. Phosphorylase kinase b
    3. Inhibitor-1
    4. All of the above
(Ref. 1, pp. 204-205)
  1. Cyclic AMP binds to:
    1. Catalytic subunits of protein kinase A
    2. Regulatory subunits of protein kinase A
    3. Catalytic subunits of phosphorylase kinase
    4. Regulatory subunits of phosphorylase kinase
(Ref. 1, p. 202)
  1. Glucose is the only source of energy for:
    1. Myocardium
    2. Kidneys
    3. Erythrocytes
    4. Thrombocytes
(Ref. 1, p. 190)
  1. Glycerol-3-phosphate for the synthesis of triglycerides in adipose tissue is derived from:
    1. Phosphatidic acid
    2. Diacylglycerol
    3. Glycerol
    4. Glucose
(Ref. 1, p. 279)
58 D
59 C
60 C
61 D
62 B
63 C
64 D
100
  1. In anaerobic conditions, muscles can derive energy from:
    1. Fatty acids
    2. Amino acids
    3. Glucose
    4. All of the above
(Ref. 1, p. 208)
  1. Gluconeogenesis occurs in:
    1. Adipose tissue
    2. Muscles
    3. Kidneys
    4. Brain
(Ref. 1, p.208)
  1. Glucose cannot be synthesised from:
    1. Glutamate
    2. Aspartate
    3. Alanine
    4. Leucine
(Ref. 1, p. 324)
  1. Reactions of gluconeogenesis occur in:
    1. Cytosol only
    2. Mitochondria only
    3. Cytosol and mitochondria
    4. Cytosol and microsomes
(Ref. 1, pp. 208-209)
  1. Coenzyme for phosphoenolpyruvate carboxykinase is:
    1. ATP
    2. ADP
    3. GTP
    4. GDP
(Ref. 1, p. 208)
  1. Pyruvate carboxylase is present in:
    1. Cytosol
    2. Mitochondria
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 208)
  1. Synthesis of one molecule of glucose from two molecules of pyruvate is accompanied by oxidation of:
    1. One molecule of NADPH
    2. One molecule of NADH
    3. Two molecules of NADPH
    4. Two molecules of NADH
(Ref. 1, p.209)
  1. Energy spent during synthesis of one molecule of glucose from two molecules of lactate is:
    1. 2 ATP equivalents
    2. 4 ATP equivalents
    3. 6 ATP equivalents
    4. 10 ATP equivalents
(Ref. 1, p. 209)
65 C
66 C
67 D
68 C
69 C
70 B
71 D
72 C
101
  1. During synthesis of one molecule of glucose from two molecules of glycerol, two molecules of:
    1. NADPH are oxidised
    2. NADH are oxidised
    3. NADP are reduced
    4. NAD are reduced
(Ref. 1, p.209)
  1. A gluconeogenic enzyme among the following is:
    1. Phosphofructokinase
    2. Pyruvate kinase
    3. Phosphoenol pyruvate carboxykinase
    4. Glucokinase
(Ref. 1, p. 209)
  1. Glucose-6-phosphatase and PEP carboxykinase are regulated by:
    1. Covalent modification
    2. Allosteric regulation
    3. Induction and repression
    4. All of the above
(Ref. 1, p. 212)
  1. Regulation of gluconeogenesis is reciprocal to that of:
    1. Glycogenesis
    2. Glycogenolysis
    3. Glycolysis
    4. HMP shunt
(Ref. 1, p. 211)
  1. Gluconeogenesis is decreased by:
    1. Glucagon
    2. Epinephrine
    3. Glucocorticoids
    4. Insulin
(Ref. 1, p. 212)
  1. Lactate formed in muscles can be utilised through:
    1. Rapoport-Luebering cycle
    2. Glucose-alanine cycle
    3. Cori cycle
    4. Citric acid cycle
(Ref. 1, p. 214)
  1. Pyruvate formed in muscles can be used for gluconeogenesis in liver through:
    1. Rapoport-Luebering cycle
    2. B. Glucose-alanine cycle
    3. Cori cycle
    4. Citric acid cycle
(Ref. 1, p. 214)
73 D
74 C
75 C
76 C
77 D
78 C
79 B
102
  1. Glucose-6-phosphatase is not present in:
    1. Liver and kidneys
    2. Kidneys and muscles
    3. Kidneys and adipose tissue
    4. Muscles and adipose tissue
(Ref. 1, p. 210)
  1. Cobamides are required as coenzymes for gluconeogenesis from:
    1. Lactate
    2. Pyruvate
    3. Succinyl CoA
    4. Propionyl CoA
(Ref. 1, p. 210)
  1. Pyruvate carboxylase is regulated by:
    1. Induction
    2. Repression
    3. Allosteric regulation
    4. All of the above
(Ref. 1, p. 212)
  1. Fructose-1, 6-biphosphatase is regulated by:
    1. Induction
    2. Repression
    3. Allosteric regulation
    4. All of the above
(Ref. 1, pp. 212-213)
  1. Fructose-2, 6-biphosphate is an allosteric regulator of:
    1. Phosphofructokinase
    2. Fructose-1, 6-biphosphatase
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 213)
  1. Fructose-2, 6-biphosphate is formed by the action of:
    1. Phosphofructokinase-1
    2. Phosphofructokinase-2
    3. Fructose biphosphate isomerase
    4. Fructose-1, 6-biphosphatase
(Ref. 1, p. 213)
  1. Phosphofructokinase-2 is regulated by:
    1. Allosteric mechanism and induction
    2. Covalent modification and allosteric mechanism
    3. Induction and repression
    4. Repression and derepression
(Ref. 1, p. 213)
80 D
81 D
82 D
83 D
84 C
85 B
86 B
103
  1. The coenzyme for UDP-glucose dehydrogenase is:
    1. NAD
    2. NADP
    3. FAD
    4. Lipoic acid
(Ref. 1, p. 224)
  1. UDP-Glucuronic acid is needed to synthesise:
    1. Hyaluronic acid
    2. Chondroitin sulphate
    3. Heparin
    4. All of the above
(Ref. 1, p. 223)
  1. In the polyol pathway, glucose is converted into:
    1. Glycerol
    2. Dulcitol
    3. Sorbitol
    4. Mannitol
(Ref. 1, p. 228)
  1. The highest concentrations of fructose are found in:
    1. Aqueous humor
    2. Vitreous humor
    3. Synovial fluid
    4. Seminal fluid
(Ref. 1, p. 226)
  1. Glucose uptake by liver cells is:
    1. Energy-dependent
    2. Mediated by GLUT4
    3. Sodium-dependent
    4. Insulin-independent
(Ref. 1, pp. 215-216)
  1. Maximum capacity for tubular reabsorption of glucose is about:
    1. 180mg/dl
    2. 180mg/min
    3. 350mg/dl
    4. 350 mg/min
(Ref. 1, p. 217)
  1. A decrease in tubular reabsorption of glucose results in:
    1. Hypoglycaemia
    2. Hyperglycaemia
    3. Renal glycosuria
    4. Alimentary glycosuria
(Ref. 1, p.217)
  1. Active uptake of glucose by renal tubules is inhibited by:
    1. Ouabain
    2. Phlorrizin
    3. Digoxin
    4. Alloxan
(Ref. 1. p.217)
  1. Insulin receptors are down-regulated in:
    1. Insulin-dependent diabetes mellitus
    2. Protein deficiency
    3. Starvation
    4. Obesity
(Ref. 1, p. 622)
87 A
88 D
89 C
90 D
91 D
92 D
93 C
94 B
95 D
104
  1. Glucose-6-phosphatase is absent or deficient in:
    1. von Gierke's disease
    2. Pompe's disease
    3. Con's disease
    4. McArdle's disease
(Ref. 1, p. 206)
  1. Debranching enzyme is absent in:
    1. Con's disease
    2. Andersen's disease
    3. von Gierke's disease
    4. Her's disease
(Ref. 1, p. 206)
  1. Amylopectinosis occurs due to absence or deficiency of:
    1. Phosphorylase
    2. Glycogen synthetase
    3. Branching enzyme
    4. Debranching enzyme
(Ref. 1, p. 206)
  1. In congenital absence of debranching enzyme:
    1. Amylopectin is deposited in tissues
    2. Limit dextrin is deposited in tissues
    3. Glycogen accumulates in tissues
    4. Glycogen stores are decreased
(Ref. 1, p. 206)
  1. Congenital phosphofructokinase deficiency causes:
    1. Hypoglycaemia
    2. Ketosis
    3. Diminished exercise tolerance
    4. All of the above
(Ref. 1, p. 206)
  1. McArdle's disease is due to deficiency of:
    1. Glucose-6-phosphatase
    2. Phosphofructokinase
    3. Liver phosphorylase
    4. Muscle phosphorylase
(Ref. 1, p. 206)
  1. Congenital galactosaemia is due to absence or deficiency of:
    1. Lactose synthetase
    2. Galactgsose-1-phosphate uridyl transferase
    3. Hexokinase
    4. Aldose reductase
(Ref. 1, p. 229)
96 A
97 A
98 C
99 B
100 C
101 D
102 B
105
  1. Hereditary fructose intolerance occurs due to absence or deficiency of:
    1. Fructokinase
    2. Fructose-1, 6-biphosphatase
    3. Aldolase
    4. Aldolase B
(Ref. 1, p. 225)
  1. Fructokinase is congenitally absent in:
    1. Hereditary fructose intolerance
    2. Fructosaemia
    3. Essential fructosuria
    4. Her's disease
(Ref. 1, p. 225)
  1. In essential pentosuria, urine contains:
    1. D-Ribose
    2. D-Xylulose
    3. L-Xylulose
    4. D-Xylose
(Ref. 1, p. 224)
  1. Hurler's syndrome is due to deficiency of:
    1. α-L-Iduronidase
    2. Iduronate sulphatase
    3. β-Galactosidase
    4. Alylsulphatase A
(Ref. 1, p. 705)
  1. Action of salivary amylase on starch leads to the formation of:
    1. Maltose
    2. Maltotriose
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 668)
  1. Glucose-6-phosphate and glucose-1-phosphate can be interconverted by:
    1. Glucose phosphate isomerase
    2. Phosphohexose isomerase
    3. Glucose phosphate racemase
    4. Phosphoglucomutase
(Ref. 1, p. 199)
  1. Congenital galactosaemia can lead to:
    1. Mental retardation
    2. Premature cataract
    3. Death
    4. All of the above
(Ref. 2, p. 493)
103 D
104 C
105 C
106 A
107 C
108 D
109 D
106
  1. Uridine diphosphate glucose (UDPG) is:
    1. Required for metabolism of galactose
    2. Required for synthesis of glucuronic acid
    3. A substrate for glycogen synthetase
    4. All of the above
(Ref. 1, pp. 199, 224, 226)
  1. Hexose monophosphate shunt provides:
    1. Glucose-1-phosphate for glycogen synthesis
    2. Glycerol-3-phosphate for triglyceride synthesis
    3. NADPH for fatty acid synthesis
    4. Glucuronic acid for mucopolysaccharide synthesis
(Ref. 1, pp.220-221)
  1. Glycogenesis requires:
    1. Uridine diphosphate glucose
    2. Glycogen synthetase
    3. Branching enzyme
    4. All of the above
(Ref. 1, p. 200)
  1. Catalytic activity of salivary amylase requires the presence of:
    1. Chloride ions
    2. Bromide ions
    3. Iodide ions
    4. Any of the above three
(Ref. 1, p. 668)
  1. Disaccharides can be hydrolysed by enzymes present in:
    1. Saliva
    2. Pancreatic juice
    3. Bile
    4. Succus entericus
(Ref. 1, pp. 668-669)
  1. The following is actively absorbed in the intestine:
    1. Fructose
    2. Mannose
    3. Galactose
    4. None of the above
(Ref. 1, p. 667)
  1. An amphibolic pathway among the following is:
    1. HMP shunt
    2. Glycolysis
    3. Citric acid cycle
    4. Gluconeogenesis
(Ref. 1, p. 187)
110 D
111 C
112 D
113 A
114 D
115 C
116 C
107
  1. A reaction of glycolytic pathway which is spontaneous is the conversion of:
    1. Glucose-6-phosphate into fructose-6-phosphate
    2. 3-Phosphoglycerate into 2-phosphoglycerate
    3. 2-Phosphoglycerate into enolpyruvate
    4. Enolpyruvate into pyruvate
(Ref. 1, p. 192)
  1. GTP is required in the reaction catalysed by:
    1. Pyruvate carboxylase
    2. PEP carboxykinase
    3. Fructose-1, 6-biphosphatase
    4. Glucose-6-phosphatase
(Ref. 1, p. 209)
  1. ATP is required in the reaction catalysed by:
    1. Pyruvate carboxylase
    2. PEP carboxykinase
    3. Fructose-1, 6-biphosphatase
    4. Glucose-6-phosphatase
(Ref. 1, p. 209)
  1. For the synthesis of hexosamines, amino group is provided by:
    1. Ammonia
    2. Glutamate
    3. Glutamine
    4. Asparagine
(Ref. 1, p. 228)
  1. Deficiency or inhibition of fructose-1, 6-biphosphatase is expected to impair:
    1. Utilisation of dietary fructose
    2. Oxidation of glucose to pyruvate
    3. Synthesis of glucose from pyruvate
    4. None of the above
(Ref. 1, p. 209)
  1. Intestinal digestion of lactose yields:
    1. Glucose and galactose
    2. Glucose and fructose
    3. Glucose and mannose
    4. Galactose and mannose
(Ref. 1, p. 669)
  1. The substrate for invertase is:
    1. Lactose
    2. Maltose
    3. Sucrose
    4. Dextrin
(Ref. 2, p. 471)
117 D
118 B
119 A
120 C
121 C
122 A
123 C
108
  1. Lactose intolerance can occur due to deficiency of:
    1. Galactokinase
    2. UDP-galactose-4-epimerase
    3. Galactose-1-phosphate uridyl transferase
    4. Lactase
(Ref. 1, p. 672)
  1. Sorbitol can be formed from:
    1. Glucose
    2. Galactose
    3. Mannose
    4. Ribose
(Ref. 1, p. 228)
  1. All the following statements about phosphofructokinase are true except:
    1. Its [S] versus velocity plot is hyperbolic at low ATP concentration
    2. Its [S] versus velocity plot is sigmoidal at high ATP concentration
    3. A rise in ATP concentration lowers the Km of the enzyme for fructose-6-phosphate
    4. AMP is its allosteric activator
(Ref. 2, p. 493)
  1. All the following statements about fructose-2, 6-biphosphate are true except:
    1. It is formed from fructose-1, 6-biphosphate
    2. It is degraded to fructose-6-phosphate
    3. It activates phosphofructokinase
    4. It inhibits fructose-1, 6-biphosphatase
(Ref. 1, p. 213)
  1. ATP decreases the activity of all of the following except:
    1. Phosphofructokinase-1
    2. Pyruvate kinase
    3. Fructose-1, 6-biphosphatase
    4. Pyruvate dehydrogenase
(Ref. 1, p. 212)
  1. Insulin increases the synthesis of all of the following except:
    1. Glucose-6-phosphatase
    2. Glucose-6-phosphate dehydrogenase
    3. 6-Phosphogluconate dehydrogenase
    4. ATP-citrate lyase
(Ref. 1, p. 212)
124 D
125 A
126 C
127 A
128 C
129 A
109
  1. Insulin represses the synthesis of all of the following except:
    1. Pyruvate carboxylase
    2. PEP carboxykinase
    3. Fructose-1, 6-biphosphatase
    4. Phosphofructokinase-1
(Ref. 1, p. 212)
  1. Glucokinase differs from hexokinase in the following respect:
    1. It has greater substrate specificity
    2. It has lower Km for glucose
    3. It acts mainly in fasting state
    4. It is inhibited by glucose-6-phosphate
(Ref. 1, p. 191)
  1. Con cycle transfers:
    1. Glucose from muscles to liver
    2. Lactate from muscles to liver
    3. Lactate from liver to muscles
    4. Pyruvate from liver to muscles
(Ref. 1, p. 214)
  1. Inorganic phosphate is required as a reactant in the reaction catalysed by:
    1. Hexokinase
    2. Phosphofructokinase
    3. Glyceralehyde-3-phosphate dehydrogenase
    4. Enolase
(Ref. 1, p. 192)
  1. Excessive intake of ethanol increases the ratio:
    1. NADH: NAD+
    2. NAD+: NADH
    3. FADH2: FAD
    4. FAD: FADH2
(Ref. 1, p. 278)
  1. Ethanol decreases gluconeogenesis by:
    1. Inhibiting glucose-6-phosphatase
    2. Inhibiting PEP carboxykinase
    3. Converting NAD+ into NADH and decreasing the availability of pyruvate
    4. Converting NAD+ into NADH and decreasing the availability of lactate
(Ref. 6, p. 99)
130 D
131 A
132 B
133 C
134 A
135 C
110
  1. Glycogenin is:
    1. Uncoupler of oxidative phosphorylation
    2. Polymer of glycogen molecules
    3. Protein primer for glycogen synthesis
    4. Intermediate in glycogen breakdown
(Ref. 1, p. 199)
  1. Glucosylation occurs at the following residue of glycogenin:
    1. Tyrosine
    2. Serine
    3. Threonine
    4. Hydroxyproline
(Ref. 1, p. 199)
  1. Oligosaccharide-pyrophosphoryl dolichol is required for the synthesis of:
    1. N-linked glycoproteins
    2. O-linked glycoproteins
    3. GPI-linked glycoproteins
    4. All of the above
(Ref. 1, p. 682)
  1. In O-linked glycoproteins, oligosaccharide is attached to protein through a:
    1. Serine or threonine residue
    2. Tyrosine residue
    3. Hydroxyproline residue
    4. Hydroxylysine residue
(Ref. 1, p. 681)
  1. In N-linked glycoproteins, oligosaccharide is attached to protein through its:
    1. Asparagine residue
    2. Glutamine residue
    3. Arginine residue
    4. Lysine residue
(Ref. 1, p. 681)
  1. Apart from liver, glucokinase is present in:
    1. Intestinal mucosa
    2. Pancreatic islet cells
    3. Renal tubular cells
    4. Erythrocytes
(Ref. 1, p.191)
136 C
137 A
138 A
139 A
140 A
141 B
111
  1. Glycolyis in erythrocytes is anaerobic because:
    1. NADH is used to reduce glutathione in erythrocytes
    2. Erythrocytes lack mitochondria
    3. Oxygen is bound to haemoglobin in erythrocytes
    4. 2,3-Biphosphoglycerate is bound to haemoglobin in mitochondria
(Ref. 1, p.191)
  1. ATP is converted into ADP in reactions catalysed by:
    1. Hexokinase and pyruvate kinase
    2. Phosphofructokinase and phosphoglycerate kinase
    3. Hexokinase and phosphofructokinase
    4. Phosphoglycerate kinase and pyruvate kinase
(Ref. 1, p.192)
  1. ADP is converted into ATP in reactions catalysed by:
    1. Hexokinase and pyruvate kinase
    2. Phosphofructokinase and phosphoglycerate kinase
    3. Hexokinase and phosphofructokinase
    4. Phosphoglycerate kinase and pyruvate kinase
(Ref. 1, p.192)
  1. During dehydrogenation of glyceraldehyde-3-phosphate, reducing equivalents are accepted by:
    1. NAD
    2. NADP
    3. FMN
    4. FAD
(Ref. 1, p.192)
  1. Iodoacetate inhibits:
    1. Aldolase
    2. Glyceraldehyde-3-phosphate dehydrogenase
    3. Phophoglycerate mutase
    4. Enolase
(Ref. 1, p.192)
  1. If glycolysis occurs in the presence of arsenate:
    1. Glyceraldehyde-3-phosphate dehydrogenase is inhibited
    2. Phosphoglycerate kinase is inhibited
    3. 1-Arseno-3-phosphoglycerate is formed
    4. Energy yield remains unaffected
(Ref. 1, p.194)
142 B
143 C
144 D
145 A
146 B
147 C
112
  1. All the following statements about biphosphoglycerate mutase and 2,3-biphosphoglycerate kinase are correct except:
    1. They catalyse reversible reactions
    2. They are present in erythrocytes
    3. Their sequential action bypasses phosphoglycerate kinase
    4. These two activities are present in the same enzyme
(Ref. 1, p.195)
  1. Energy is spent in the following phase of glycolysis:
    1. Glucose → → Fructose-1,6-biphosphate
    2. Fructose-1,6-biphosphate → Glyceraldehyde-3-phosphate + Dihydroxyacetone phosphate
    3. Glyceraldehyde-3-phosphate → →Pyruvate
    4. All of the above
(Ref. 1, p.192)
  1. Energy is captured in the following phase of glycolysis:
    1. Glucose → →Fructose-1,6-biphosphate
    2. Fructose-1, 6-biphosphate → Glyceraldehyde-3-phosphate + Dihydroxyacetone phosphate
    3. Glyceraldehyde-3-phosphate → → Pyruvate
    4. All of the above
(Ref. 1, p.192)
  1. The enzyme which splits a 6-carbon compound into two 3-carbon compounds in glycolysis is:
    1. Enolase
    2. Phosphotriose isomerase
    3. Aldolase
    4. Phosphoglycerate mutase
(Ref. 1, p.192)
  1. The correct sequence of intermediates in glycolysis is:
    1. 1,3-Biphosphoglycerate → 3-Phosphoglycerate → 2-Phosphoglycerate → Phosphoenolpyruvate
    2. 1,3-Biphosphoglycerate → 2-Phosphoglycerate → 3-Phosphoglycerate → Phosphoenolpyruvate
    3. 1,3-Biphosphoglycerate → Phosphoenolpyruvate → 2-Phosphoglycerate → 3-Phosphoglycerate
    4. Phosphoenolpyruvate → 1,3-Biphosphoglycerate → 3-Phosphoglycerate → 2-Phosphoglycerate
(Ref. 1, p.192)
148 A
149 A
152 A
113
  1. Glucose-1,6-biphosphate is formed as an intermediate during the reaction catalysed by:
    1. Glucokinase
    2. UDP-Glucose pyrophosphorylase
    3. Phosphoglucomutase
    4. Glucose-6-phosphatase
(Ref. 1, p.199)
  1. Glycogen synthetase a is phosphorylated by:
    1. cAMP-dependent protein kinase
    2. Calmodulin-dependent protein kinase
    3. Glycogen synthetase kinase
    4. All of the above
(Ref. 1, p.205)
  1. The regulatory enzyme in glycogenesis is:
    1. UDP-Glucose pyrophosphorylase
    2. Glycogen synthetase
    3. Branching enzyme
    4. All of the above
(Ref. 1, p.201)
  1. The regulatory enzyme in glycogenolysis is:
    1. Phosphorylase
    2. Glucan transferase
    3. Debranching enzyme
    4. Glucose-6-phosphatase
(Ref. 1, p.201)
  1. Regulation of glycogenesis and glycogenolysis is:
    1. Synchronous
    2. Reciprocal
    3. Mediated by cAMP
    4. All of the above
(Ref. 1, p.206)
  1. Between meals, blood glucose level can be maintained by:
    1. Glycogenolysis in liver
    2. Glycogenolysis in muscles
    3. Both of the above
    4. Neither of the above
(Ref. 1, p.201)
153 C
154 D
155 B
156 A
157 D
158 A
114
  1. A difference between phosphorylase and debranching enzyme is:
    1. Phosphorylase acts on α-1, 6 bonds while debranching enzyme acts on α-1,4 bonds
    2. Phosphorylase liberates free glucose while debranching enzyme liberates glucose-1-phosphate
    3. Debranching enzyme catalyses the rate-limiting step of glycogenolysis while phosphorylase does not
    4. None of the above
(Ref. 1, p.201)
  1. Inorganic phosphate is required as a reactant in the reaction catalysed by:
    1. Glycogen synthetase
    2. Branching enzyme
    3. Phosphorylase
    4. Debranching enzyme
(Ref. 1, p.200)
  1. Glucagon can affect the rate of glycogenesis and glycogenolysis in:
    1. Liver and skeletal muscle
    2. Liver and heart muscle
    3. Skeletal and heart muscles
    4. Liver only
(Ref. 1, p.200)
  1. In liver:
    1. Glycogenin is present in the centre of each glycogen molecule
    2. Glycogenin is not required for glycogenesis
    3. The number of glycogenin molecules exceeds the number of glycogen molecules
    4. The number of glycogen molecules exceeds the number of glycogenin molecules
(Ref. 1, p.199)
  1. All the following statements about pyruvate carboxylase are correct except:
    1. It takes part in gluconeogenesis
    2. It is present in mitochondria
    3. It is activated by acetyl CoA
    4. It is inhibited by ATP
(Ref. 1, p.209)
159 D
160 C
161 B
162 D
163 D
115
  1. All the following enzymes are required to convert lactate into phosphoenolpyruvate except:
    1. Pyruvate kinase
    2. Pyruvate carboxylase
    3. Phosphoenolpyruvate carboxykinase
    4. Lactate dehydrogenase
(Ref. 1, p.208)
  1. All the following enzymes are required to synthesise glucose from oxaloacetate except:
    1. Pyruvate carboxylase
    2. Phosphoenolpyruvate carboxykinase
    3. Fructose-1, 6-biphosphatase
    4. Glucose-6-phosphatase
(Ref. 1, p.209)
  1. All the following enzymes are required to synthesise glucose from glycerol except:
    1. Glycerol-3-phosphate dehydrogenase
    2. Phosphoenolpyruvate carboxykinase
    3. Fructose-1, 6-biphosphatase
    4. Glucose-6-phosphatase
(Ref. 1, p.209)
  1. Energy bathers for gluconeogenesis include all the following except:
    1. Pyruvate to phosphoenolpyruvate
    2. 3-Phosphoglycerate to 1,3-biphosphoglycerate
    3. Fructose-1, 6-biphosphate to fructose-6-phosphate
    4. Glucose-6-phosphate to glucose
(Ref. 1, p.208)
  1. A simple reversal of glycolysis to synthesise glucose from pyruvate or lactate is not possible because:
    1. Free energy is liberated in some of the glycolytic reactions
    2. Glycolysis and gluconeogenesis occur in different tissues
    3. Glycolysis and gluconeogenesis occur in different compartments of the cell
    4. All of the above
(Ref. 1, p.208)
  1. Gluconeogenic enzymes:
    1. Circumvent the energy barriers in glycolysis
    2. Are present in mitochondria
    3. Catalyse endergonic reactions
    4. Are regulated by covalent modification
(Ref. 1, pp.208-210)
164 A
165 A
166 B
167 B
168 A
169 A
116
  1. Energy is spent in the gluconeogenic reactions catalysed by:
    1. Pyruvate carboxylase and fructose-1, 6-biphosphatase
    2. Glucose-6-phosphatase and fructose-1,6-biphosphatase
    3. Pyruvate carboxylase and phosphoenolypyruvate carboxykinase
    4. Glucose-6-phosphatase and phosphoenolpyruvate carboxykinase
(Ref. 1, p.208)
  1. Fructose-1,6-biphosphatase is inhibited by all of the following except:
    1. Fructose-1,6-biphosphate
    2. Fructose-2,6-biphosphate
    3. ATP
    4. AMP
(Ref. 1, p.209)
  1. Glucose-6-phosphatase is allosterically inhibited by:
    1. Glucose
    2. Glucose-6-phosphate
    3. ATP
    4. None of the above
(Ref. 1, p.212)
  1. In human beings, phosphoenolpyruvate carboxykinase is present in:
    1. Cytosol
    2. Mitochondria
    3. Both of the above
    4. Neither of the above
(Ref. 1, p.210)
  1. Fructose-1, 6-biphosphatase is present in all of the following except:
    1. Liver
    2. Kidney
    3. Striated muscle
    4. Smooth muscle
(Ref. 1, p.210)
  1. A bifunctional enzyme that plays an important role in regulation of glycolysis and gluconeogenesis possesses the following catalytic activities:
    1. Glucokinase and glucose-6-phosphatase
    2. Phosphofructokinase-1 and fructose-1,6-biphosphatase
    3. Phosphofructokinase-2 and fructose-2,6-biphosphatase
    4. Pyruvate kinase and phosphoenolpyruvate carboxykinase
(Ref. 1, p.213)
170 C
171 C
172 D
173 C
174 D
175 C
117
  1. cAMP-dependent protein kinase phosphorylates and:
    1. Inactivates pyruvate kinase
    2. Activates fructose-2,6-biphosphatase
    3. Inactivates phosphofructokinase-2
    4. All of the above
(Ref. 1, pp.211, 213)
  1. All the following statements about sodium-dependent glucose transporter (SGLT 1) are correct except:
    1. It is present in muscles and adipose tissue
    2. It causes active uptake of glucose against its concentration gradient
    3. It transports sodium down its concentration gradient
    4. It is insulin-independent
(Ref. 1, pp. 215, 667)
  1. Glucose transporter present in small intestine is:
    1. SGLT 1
    2. GLUT 2
    3. GLUT 5
    4. All of the above
(Ref. 1, p.215)
  1. Fructose is absorbed in the small intestine through:
    1. SGLT 1
    2. GLUT 3
    3. GLUT 4
    4. GLUT 5
(Ref. 1, p.669)
  1. All the following statements about intestinal fructose absorption are correct except:
    1. It is absorbed by facilitated diffusion
    2. Its absorption depends upon sodium gradient
    3. It enters the mucosal cell through GLUT 5
    4. It enters the capillaries from mucosal cells through GLUT 2
(Ref. 1,pp.667)
  1. All the following statements about intestinal glucose absorption are correct except:
    1. It is absorbed against its concentration gradient
    2. Rate of its absorption is proportional to sodium gradient
    3. Its active absorption is enhanced by insulin
    4. Energy is spent during active uptake of glucose to expel sodium ions
(Ref. 1, pp. 529, 667)
176 D
177 A
178 D
179 D
180 B
181 C
118
  1. Uptake of glucose by muscles:
    1. Occurs by an active transport mechanism
    2. Is energy-dependent
    3. Is linked to sodium uptake
    4. Is enhanced by insulin
(Ref. 1, pp. 215, 216)
  1. GLUT 4:
    1. Is present in adipose tissue
    2. Facilitates diffusion of glucose
    3. Is transferred from cytosol to the cell membrane by insulin
    4. All of the above
(Ref. 1, pp. 215, 216)
  1. All the following statements about GLUT 4 are correct except:
    1. It is present in muscles and adipose tissue
    2. It is a trans-membrane protein
    3. It mediates energy-dependent uptake of glucose
    4. Number of GLUT 4 molecules in the cell membrane is increased by insulin
(Ref. 1, pp. 215, 216)
  1. A coenzyme required by transketolase as well as pyruvate dehydrogenase complex is:
    1. Thiamin pyrophosphate
    2. Lipoic acid
    3. FAD
    4. NAD
(Ref. 1, pp. 195, 221)
  1. Glycolysis and HMP shunt have the following similarity:
    1. Glucose-6-phosphate is an intermediate in both
    2. Ribose-5-phosphate is an intermediate in both
    3. NAD is reduced in both
    4. ATP is formed in both
(Ref. 1, p. 221)
  1. Intermediates common to glycolysis and HMP shunt include all of the following except:
    1. Glucose-6-phosphate
    2. Xylulose-5-phosphate
    3. Glyceraldehyde-3-phosphate
    4. Fructose-6-phosphate
(Ref. 1, pp. 192, 222)
182 D
183 D
184 C
185 A
186 A
187 B
119
  1. Fructose-6-phosphate and glyceraldehyde-3-phosphate formed in the glycolytic pathway can be used to synthesise ribose-5-phosphate if the following enzymes are also present in the cell:
    1. Transketolase and transaldolase
    2. Transketolase and ribose-5-phosphate ketoisomerase
    3. Transaldolase and ribose-5-phosphate ketoisomerase
    4. Transaldolase and ribulose-5-phosphate 3-epimerase
(Ref. 1, pp.221-223)
  1. NADPH formed in HMP shunt in erythrocytes can be used to detoxify hydrogen peroxide if the following is available:
    1. Glutathione
    2. Glutathione reductase
    3. Glutathione peroxidase
    4. All of the above
(Ref. 1, p. 223)
  1. All the following statements about fructokinase are correct except:
    1. It is present in liver
    2. It has a low Km for fructose
    3. It converts fructose into fructose-6-phosphate
    4. Its activity is not affected by insulin
(Ref. 1, p.225)
  1. Acute loading of liver with fructose may cause all of the following except:
    1. Fructosaemia
    2. Hypertriglyceridaemia
    3. Hypercholesterolaemia
    4. Hyperuricaemia
(Ref. 1, p.227)
  1. Cataract occurs in congenital galactosaemia due to accumulation of the following in lens:
    1. Galactose
    2. Galactose- 1-phosphate
    3. Galactitol
    4. Sorbitol
(Ref. 1, p.229)
  1. Normal range of fasting plasma glucose is:
    1. 65-110 mmol / litre
    2. 65-110 mg / dl
    3. 80-120 mmol / litre
    4. 80-120 mg / dl
(Ref. 1, p.869)
188 A
189 D
190 C
191 A
192 C 1
93 B
120
  1. A unidirectional transporter of glucose is:
    1. GLUT 2
    2. GLUT 3
    3. GLUT 4
    4. SGLT 1
(Ref. 1, p. 215)
  1. Blood glucose level is increased by all of the following except:
    1. Glucagon
    2. Glucocorticoids
    3. Insulin
    4. Epinephrine
(Ref. 1, p. 216)
194 D
195 C

Metabolism of Lipids12

  1. De novo synthesis of fatty acids occurs in:
    1. Cytosol
    2. Mitochondria
    3. Microsomes
    4. All of the above
(Ref. 1, p. 230)
  1. Acyl carrier protein contains the vitamin:
    1. Biotin
    2. Lipoic acid
    3. Pantothenic acid
    4. Folic acid
(Ref. 1, p. 230)
  1. The following is required as a reductant in fatty acid synthesis:
    1. NADH
    2. NADPH
    3. FADH2
    4. FMNH2
(Ref. 1, p. 230)
  1. Hepatic lipogenesis is stimulated by:
    1. cAMP
    2. Glucagon
    3. Epinephrine
    4. Insulin
(Ref. 1, p. 230)
  1. De novo synthesis of fatty acids requires all of the following except:
    1. Biotin
    2. NADH
    3. Pantothenic acid
    4. ATP
(Ref. 1, p. 230)
  1. Acetyl CoA carboxylase regulates fatty acid synthesis by the following mechanism:
    1. Allosteric regulation
    2. Covalent modification
    3. Induction and repression
    4. All of the above
(Ref. 1, p. 237)
1 A
2 C
3 B
4 D
5 B
6 D
122
  1. β-Oxidation of fatty acids requires all the following coenzymes except:
    1. CoA
    2. FAD
    3. NMD
    4. NADP
(Ref. 1, pp. 240-241)
  1. The following can be oxidised by β-oxidation pathway:
    1. Saturated fatty acids
    2. Monounsaturated fatty acids
    3. Polyunsaturated fatty acids
    4. All of the above
(Ref. 1, pp. 239-240, 242)
  1. Propionyl CoA is formed on oxidation of:
    1. Monounsaturated fatty acids
    2. Polyunsaturated fatty acids
    3. Fatty acids with odd number of carbon atoms
    4. None of the above
(Ref. 1, p. 240)
  1. An enzyme required for the synthesis of ketone bodies as well as cholesterol is:
    1. Acetyl CoA carboxylase
    2. HMG CoA synthetase
    3. HMG CoA reductase
    4. HMG CoA lyase
(Ref. 1, pp. 244, 286)
  1. Ketone bodies are synthesised in:
    1. Adipose tissue
    2. Liver
    3. Muscles
    4. Brain
(Ref. 1, p. 243)
  1. All the following statements about ketone bodies are true except:
    1. Their synthesis increases in diabetes mellitus
    2. They are synthesised in mitochondria
    3. They can deplete the alkali reserve
    4. They can be oxidised in the liver
(Ref. 1, pp. 243, 248)
7 D
8 D
9 C
10 B
11 B
12 D
123
  1. All the following statements about carnitine are true except:
    1. It can be synthesised in the human body
    2. It can be synthesised from methionine and lysine
    3. It is required for transport of short chain fatty acids into mitochondria
    4. Its deficiency can occur due to haemodialysis
(Ref. 1, pp. 239, 247)
  1. The following can be synthesised in the human body if precursors are available:
    1. Oleic acid
    2. Palmitoleic acid
    3. Arachidonic acid
    4. All of the above
(Ref. 1, p. 250)
  1. All the following can be oxidised by β-oxidation except:
    1. Palmitic acid
    2. Phytanic acid
    3. Linoleic acid
    4. Fatty acids having an odd number of carbon atoms
(Ref. 1, pp. 240-242, 248)
  1. Anti-inflammatory corticosteroids inhibit the synthesis of:
    1. Prostacyclins
    2. Prostaglandins
    3. Thromboxanes
    4. All of the above
(Ref. 1, p. 254)
  1. Diets having a high ratio of polyunsaturated: saturated fatty acids can cause:
    1. Increase in serum triglycerides
    2. Decrease in serum cholesterol
    3. Decrease in serum HDL
    4. Skin lesions
(Ref. 1, p. 250)
  1. Thromboxanes cause:
    1. Vasodilation
    2. Bronchoconstriction
    3. Platelet aggregation
    4. All of the above
(Ref. 1, p. 257)
13 C
14 D
15 B
16 D
17 B
18 C
124
  1. Prostaglandins lower cAMP in:
    1. Adipose tissue
    2. Lungs
    3. Platelets
    4. Adenohypophysis
(Ref. 1, p. 258)
  1. Slow Reacting Substance of Anaphylaxis is a mixture of:
    1. Prostaglandins
    2. Prostacyclins
    3. Thromboxanes
    4. Leukotrienes
(Ref. 1, p. 258)
  1. Dipalmitoyl lecithin acts as:
    1. Platelet activating factor
    2. Second messenger for hormones
    3. Lung surfactant
    4. Anti-ketogenic compound
(Ref. 1, p. 164)
  1. The following tissue cannot utilise glycerol as it lacks glycerol kinase:
    1. Liver
    2. Kidney
    3. Intestine
    4. Adipose tissue
(Ref. 1, p. 260)
  1. In glycerophospholipids, a polyunsaturated fatty acid is commonly attached to the following carbon atom of glycerol:
    1. Carbon 1
    2. Carbon 2
    3. Both of the above
    4. Neither of the above
(Ref. 1, pp. 263-264)
  1. Lysolecithin is formed from lecithin by removal of:
    1. Fatty acid from position 1
    2. Fatty acid from position 2
    3. Phosphorylcholine
    4. Choline
(Ref. 1, p. 263)
  1. Sphingosine is synthesised from:
    1. Palmitoyl CoA and choline
    2. Palmitoyl CoA and ethanolamine
    3. Palmitoyl CoA and serine
    4. Acetyl CoA and choline
(Ref. 1, p. 264)
19 A
20 D
21 C
22 D
23 B
24 B
25 C
125
  1. For synthesis of sphingosine, all the following coenzymes are required except:
    1. Pyridoxal phosphate
    2. NADPH
    3. FAD
    4. NAD
(Ref. 2, p. 689)
  1. Cerebrosides contain all of the following except:
    1. Galactose
    2. Sulphate
    3. Sphingosine
    4. Fatty acid
(Ref. 1, p. 265)
  1. Niemann-Pick disease results from deficiency of:
    1. Ceramidase
    2. Sphingomyelinase
    3. Arylsulphatase A
    4. Hexosaminidase A
(Ref. 1, p. 267)
  1. Inherited deficiency of β-glucosidase causes:
    1. Tay-Sachs disease
    2. Metachromatic leukodystrophy
    3. Gaucher's disease
    4. Multiple sclerosis
(Ref. 1, p. 267)
  1. Tay-Sachs disease results from inherited deficiency of:
    1. Arylsulphatase A
    2. Hexosaminidase A
    3. Sphingomyelinase
    4. Ceramidase
(Ref. 1, p. 267)
  1. The largest apolipoprotein is:
    1. Apo E
    2. Apo B-48
    3. Apo B-100
    4. Apo A-I
(Ref. 1, p. 270)
  1. Apolipoprotein B-100 is synthesised in:
    1. Adipose tissue
    2. Liver
    3. Intestine
    4. Liver and intestine
(Ref. 1, p. 270)
  1. Apolipoprotein B-48 is synthesised in:
    1. Adipose tissue
    2. Liver
    3. Intestine
    4. Liver and intestine
(Ref. 1, p. 270)
26 D
27 B
28 B
29 C
30 B
31 C
32 B
33 C
126
  1. Apolipoproteins A-I and A-II are present in:
    1. LDL only
    2. LDL and VLDL
    3. HDL only
    4. HDL and chylomicrons
(Ref. 1, p. 270)
  1. Apolipoprotein B-48 is present in:
    1. Chylomicrons
    2. VLDL
    3. LDL
    4. HDL
(Ref. 1, p. 270)
  1. Apolipoprotein B-100 is present in:
    1. Chylomicrons
    2. VLDL only
    3. LDL only
    4. VLDL and LDL
(Ref. 1, p. 270)
  1. Apolipoproteins C-I, C-II and C-III are present in:
    1. Chylomicrons
    2. VLDL
    3. HDL
    4. All of the above
(Ref. 1, p. 270)
  1. Apolipoproteins C-I, C-II and C-III are present in all of the following except:
    1. Chylomicrons
    2. VLDL
    3. LDL
    4. HDL
(Ref. 1, p. 270)
  1. Apolipoprotein A-I acts as:
    1. Enzyme activator
    2. Ligand for receptor
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 270)
  1. Apolipoprotein B-100 acts as:
    1. Enzyme activator
    2. Ligand for receptor
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 270)
  1. Apolipoprotein C-II is an activator of:
    1. Lecithin cholesterol acyl transferase
    2. Phospholipase C
    3. Extrahepatic lipoprotein lipase
    4. Hepatic lipoprotein lipase
(Ref. 1, p. 270)
  1. Nascent chylomicron receives apolipoproteins C and E from:
    1. VLDL remnant
    2. VLDL
    3. LDL
    4. HDL
(Ref. 1, p. 272)
34 D
35 A
36 D
37 D
38 C
39 C
40 B
41 C
42 D
127
  1. Chylomicron remnants are catabolised in:
    1. Intestine
    2. Adipose tissue
    3. Liver
    4. Liver and intestine
(Ref. 1, p. 272)
  1. VLDL remnant may be converted into:
    1. VLDL
    2. LDL
    3. HDL
    4. Chylomicrons
(Ref. 1, p. 273)
  1. Receptors for chymicron remnants are:
    1. Apo A specific
    2. Apo B-48 specific
    3. Apo C specific
    4. Apo E specific
(Ref. 1, p. 274)
  1. LDL receptor is specific for:
    1. Apo B-48 and Apo B-100
    2. Apo B-48 and Apo E
    3. Apo B-100 and Apo E
    4. Apo B-100 and Apo D
(Ref. 1, p. 274)
  1. Nascent HDL of intestinal origin lacks:
    1. Apo A
    2. Apo C
    3. Apo E
    4. Apo C and Apo E
(Ref. 1, p. 274)
  1. HDL is synthesised in:
    1. Adipose tissue
    2. Liver
    3. Intestine
    4. Liver and intestine
(Ref. 1, p. 274)
  1. Nascent HDL of intestinal origin acquires Apo C and Apo E from:
    1. Chylomicrons
    2. VLDL
    3. LDL
    4. HDL of hepatic origin
(Ref. 1, p. 275)
  1. Heparin releasable hepatic lipase converts:
    1. VLDL remnants into LDL
    2. Nascent HDL into HDL
    3. HDL2 into HDL3
    4. HDL3 into HDL2
(Ref. 1, pp. 275-276)
43 C
44 B
45 D
46 C
47 D
48 D
49 D
50 C
128
  1. Activated lecithin cholesterol acyl transferase is essential for the conversion of:
    1. VLDL remnants into LDL
    2. Nascent HDL into HDL
    3. HDL2 into HDL3
    4. HDL3 into HDL2
(Ref. 1, p. 275)
  1. Fatty liver may be caused by:
    1. Deficiency of methionine
    2. Puromycin
    3. Chronic alcoholism
    4. All of the above
(Ref. 1, p. 278)
  1. Alcohol dehydrogenase converts ethanol into:
    1. Acetyl CoA
    2. Acetaldehyde
    3. Acetate
    4. CO2 and H2O
(Ref. 1, p. 278)
  1. Lipids are stored in the body mainly in the form of:
    1. Phospholipids
    2. Glycolipids
    3. Triglycerides
    4. Fatty acids
(Ref. 1, p. 163)
  1. Lipid stores are mainly present in:
    1. Liver
    2. Brain
    3. Muscles
    4. Adipose tissue
(Ref. 1, p. 283)
  1. Glycerol is converted into glycerol-3-phosphate by:
    1. Thiokinase
    2. Triokinase
    3. Glycerol kinase
    4. All of the above
(Ref. 1, p. 261)
  1. In adipose tissue, glycerol-3-phosphate required for the synthesis of triglycerides comes mainly from:
    1. Hydrolysis of pre-existing triglycerides
    2. Hydrolysis of phospholipids
    3. Dihydroxyacetone phosphate formed in glycolysis
    4. Free glycerol
(Ref. 1, p. 260)
51 B
52 D
53 B
54 C
55 D
56 C
57 C
129
  1. Glycerol released from adipose tissue by hydrolysis of triglycerides is mainly:
    1. Taken up by liver
    2. Taken up by extrahepatic tissues
    3. Reutilised in adipose tissue
    4. Excreted from the body
(Ref. 1, p. 279)
  1. Free glycerol cannot be used for triglyceride synthesis in:
    1. Liver
    2. Kidney
    3. Intestine
    4. Adipose tissue
(Ref. 1, pp. 259-260)
  1. Adipose tissue lacks:
    1. Hormone-sensitive lipase
    2. Glycerol kinase
    3. cAMP-dependent protein kinase
    4. Glycerol-3-phosphate dehydrogenase
(Ref. 1, pp. 260, 281)
  1. A digestive secretion that does not contain any digestive enzyme is:
    1. Saliva
    2. Gastric juice
    3. Pancreatic juice
    4. Bile
(Ref. 1, p. 664)
  1. Saliva contains a lipase which is secreted by:
    1. Dorsal surface of tongue
    2. Parotid glands
    3. Sub-maxillary glands
    4. All of the above
(Ref. 1, p. 662)
  1. Gastric lipase hydrolyses the ester bond at:
    1. Position 1 of triglycerides
    2. Position 2 of triglycerides
    3. Position 3 of triglycerides
    4. All of the above
(Ref. 1, p. 663)
58 A
59 D
60 B
61 D
62 A
63 C
130
  1. Lingual lipase converts dietary triglycerides into:
    1. Diglycerides and fatty acids
    2. Monoglycerides and fatty acids
    3. Glycerol and fatty acids
    4. All of the above
(Ref. 1, p. 668)
  1. Pancreatic lipase requires for its activity:
    1. Co-lipase
    2. Bile salts
    3. Phospholipids
    4. All of the above
(Ref. 1, p. 665)
  1. Pancreatic lipase converts triacylglycerols into:
    1. 2, 3-Diacylglycerol
    2. 1-Monoacylglycerol
    3. 2-Monoacylglycerol
    4. 3-Monoacylglycerol
(Ref. 1, p. 665)
  1. Oxidation of fatty acids occurs:
    1. In the cytosol
    2. In the matrix of mitochondria
    3. On inner mitochondrial membrane
    4. On the microsomes
(Ref. 1, p. 238)
  1. Activation of fatty acids requires all the following except:
    1. ATP
    2. Coenzyme A
    3. Thiokinase
    4. Carnitine
(Ref. 1, p. 238)
  1. Mitochondrial thiokinase acts on:
    1. Short chain fatty acids
    2. Medium chain fatty acids
    3. Long chain fatty acids
    4. All of the above
(Ref. 1, p. 239)
  1. Carnitine is required for the transport of:
    1. Triglycerides out of liver
    2. Triglycerides into mitochondria
    3. Short chain fatty acids into mitochondria
    4. Long chain fatty acids into mitochondria
(Ref. 1, p. 239)
66 A
65 D
66 C
67 B
68 D
69 A
70 D
131
  1. Carnitine acylcarnitine translocase is present:
    1. In the inner mitochondrial membrane
    2. In the mitochondrial matrix
    3. On the outer surface of inner mitochondrial membrane
    4. On the inner surface of inner mitochondrial membrane
(Ref. 1, p. 239)
  1. Net ATP generation on complete oxidation of stearic acid is:
    1. 129
    2. 131
    3. 146
    4. 148
(Ref. 1, pp. 161, 240-241)
  1. Propionyl CoA formed on oxidation of fatty acids having an odd number of carbon atoms is converted into:
    1. Acetyl CoA
    2. Acetoacetyl CoA
    3. C. D-Methylmalonyl CoA
    4. Butyryl CoA
(Ref. 1, p. 210)
  1. 74. α-Oxidation of fatty acids occurs mainly in:
    1. Liver
    2. Brain
    3. Muscles
    4. Adipose tissue
(Ref. 1, p. 240)
  1. Refsum's disease results from a defect in the following pathway:
    1. Alpha-oxidation of fatty acids
    2. Beta-oxidation of fatty acids
    3. Gamma-oxidation of fatty acids
    4. Omega-oxidation of fatty acids
(Ref. 1, p. 248)
  1. The end product of omega-oxidation of fatty acids having an even number of carbon atoms is:
    1. Adipic acid
    2. Suberic acid
    3. Either of the above
    4. Neither of the above
(Ref. 1, p. 242)
71 A
72 C
73 C
74 B
75 A
76 C
132
  1. De novo synthesis of fatty acids is catalysed by a multi-enzyme complex which contains:
    1. One -SH group
    2. Two -SH groups
    3. Three -SH groups
    4. Four -SH groups
(Ref. 1, p. 231)
  1. The maximum possible chain length of fatty acids formed in the pathway of de novo synthesis is:
    1. 16 Carbon atoms
    2. 18 Carbon atoms
    3. 20 Carbon atoms
    4. 24 Carbon atoms
(Ref. 1, p. 233)
  1. Acetyl CoA required for de novo synthesis of fatty acids is obtained from:
    1. Breakdown of existing fatty acids
    2. Ketone bodies
    3. Acetate
    4. Pyruvate
(Ref. 1, p. 233)
  1. Formation of acetyl CoA from pyruvate for de novo synthesis of fatty acids requires:
    1. Pyruvate dehydrogenase complex
    2. Citrate synthetase
    3. ATP-citrate lyase
    4. All of the above
(Ref. 1, pp. 233-234)
  1. The major site for elongation of medium chain fatty acids is:
    1. Mitochondria
    2. Cytosol
    3. Microsomes
    4. All of the above
(Ref. 1, p. 235)
  1. β-Oxidation of fatty acids is inhibited by:
    1. NADPH
    2. Acetyl CoA
    3. Malonyl CoA
    4. None of the above
(Ref. 1, p. 247)
  1. The enzyme regulating extramitochondrial fatty acid synthesis is:
    1. Thioesterase
    2. Acetyl CoA carboxylase
    3. Acyl transferase
    4. Multi-enzyme complex
(Ref. 1, p. 236)
77 D
78 A
79 D
80 D
81 C
82 C
84 B
133
  1. Acetyl CoA carboxylase is activated by:
    1. Citrate
    2. Insulin
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 237)
  1. All the following statements about acetyl CoA carboxylase are true except:
    1. It is activated by citrate
    2. It is inhibited by palmitoyl CoA
    3. It can undergo covalent modification
    4. Its dephosphorylated form is inactive
(Ref. 1, p. 237)
  1. All the following statements about acetyl CoA carboxylase are true except:
    1. It is required for de novo synthesis of fatty acids
    2. It is required for mitochondrial elongation of fatty acids
    3. It is required for microsomal elongation of fatty acids
    4. Insulin converts its inactive form into its active form
(Ref. 1, pp. 235, 237)
  1. Lipogenesis is decreased in all the following except:
    1. Restricted caloric intake
    2. High fat intake
    3. Deficiency of insulin
    4. High carbohydrate intake
(Ref. 1, p.235)
  1. Co-lipase binds to:
    1. Lingual lipase
    2. Gastric lipase
    3. Pancreatic lipase
    4. All of the above
(Ref. 1, p. 655)
  1. Co-lipase is a:
    1. Bile salt
    2. Vitamin
    3. Protein
    4. Phospholipid
(Ref. 1, p. 655)
84 C
85 D
86 B
87 D
88 C
89 C
134
  1. Plasma becomes milky:
    1. Due to high level of HDL
    2. Due to high level of LDL
    3. During fasting
    4. After a meal
(Ref. 1, p. 669)
  1. Mitochondrial membrane is permeable to:
    1. Short chain fatty acids
    2. Medium chain fatty acids
    3. Long chain fatty acids
    4. All of the above
(Ref. 1, p. 239)
  1. During each cycle of α-oxidation:
    1. One carbon atom is removed from the carboxyl end of the fatty acid
    2. One carbon atom is removed from the methyl end of the fatty acid
    3. Two carbon atoms are removed from the carboxyl end of the fatty acid
    4. Two carbon atoms are removed from the methyl end of the fatty acid
(Ref. 1, p. 239)
  1. Net generation of energy on complete oxidation of palmitic acid is:
    1. 129 ATP equivalents
    2. 131 ATP equivalents
    3. 146 ATP equivalents
    4. 148 ATP equivalents
(Ref. 1, p. 240)
  1. Very long chain fatty acids are:
    1. Not oxidised
    2. Oxidised in mitochondria
    3. Oxidised in peroxisomes
    4. Present in adipose tissue
(Ref. 1, p. 240)
  1. Net energy generation on complete oxidation of linoleic acid is:
    1. 148 ATP equivalents
    2. 146 ATP equivalents
    3. 144 ATP equivalents
    4. 142 ATP equivalents
(Ref. 1, pp. 240-242)
90 D
91 A
92 C
93 A
94 C
95 D
135
  1. Extramitochondrial synthesis of fatty acids occurs in:
    1. Mammary glands
    2. Lungs
    3. Brain
    4. All of the above
(Ref. 1, p. 230)
  1. One functional sub-unit of multi-enzyme complex for de novo synthesis of fatty acids contains:
    1. One -SH group
    2. Two -SH groups
    3. Three -SH groups
    4. Four -SH groups
(Ref. 1, p. 231)
  1. NADPH required for fatty acid synthesis can come from:
    1. Hexose monophosphate shunt
    2. Oxidative decarboxylation of malate
    3. Extramitochondrial oxidation of isocitrate
    4. All of the above
(Ref. 1, p. 233)
  1. Fatty liver may be prevented by all of the following except:
    1. Choline
    2. Vitamin E
    3. Methionine
    4. Ethionine
(Ref. 1, p. 278)
  1. Human desaturase enzyme system cannot introduce a double bond in a fatty acid beyond:
    1. Carbon 9
    2. Carbon 6
    3. Carbon 5
    4. Carbon 3
(Ref. 1, p. 250)
  1. The following lipid is absorbed actively from intestines:
    1. Glycerol
    2. Cholesterol
    3. Monoacylglycerol
    4. None of the above
(Ref. 1, p. 669)
96 D
97 B
98 D
99 D
100 A
101 D
136
  1. C22 and C24 fatty acids required for the synthesis of sphingolipids in brain are formed by:
    1. De novo synthesis
    2. Microsomal chain elongation
    3. Mitochondrial chain elongation
    4. All of the above
(Ref. 1, p. 235)
  1. From the intestinal mucosa, dietary short chain fatty acids:
    1. Enter the lacteals
    2. Enter portal circulation
    3. Are converted into phospholipids
    4. Are converted into triglycerides
(Ref. 1, p. 669)
  1. All of the following statements about hypoglycin are true except:
    1. It is a plant toxin
    2. It causes hypoglycaemia
    3. It inhibits oxidation of short chain fatty acids
    4. It inhibits oxidation of long chain fatty acids
(Ref. 1, p. 248)
  1. Synthesis of prostaglandins is inhibited by:
    1. Glucocorticoids
    2. Aspirin
    3. Indomethacin
    4. All of the above
(Ref. 1, p. 254)
  1. Lipo-oxygenase is required for the synthesis of:
    1. Prostaglandins
    2. Leukotrienes
    3. Thromboxanes
    4. All of the above
(Ref. 1, p. 254)
  1. All of the following statements about multiple sclerosis are true except:
    1. There is loss of phospholipids from white matter
    2. There is loss of sphingolipids from white matter
    3. There is loss of esterified cholesterol from white matter
    4. White matter resembles gray matter in composition
(Ref. 1, pp. 265-266)
102 B
103 B
104 D
105 D
106 B
107 C
137
  1. After entering cytosol, free fatty acids are bound to:
    1. Albumin
    2. Globulin
    3. Fatty acid binding protein
    4. None of the above
(Ref. 1, p. 238)
  1. Release of free fatty acids from adipose tissue is increased by all of the following except:
    1. Glucagon
    2. Epinephrine
    3. Growth hormone
    4. Insulin
(Ref. 1, p. 281)
  1. All the following statements about brown adipose tissue are true except:
    1. It is rich in cytochromes
    2. It oxidises glucose and fatty acids
    3. Oxidation and phosphorylation are tightly coupled in it
    4. Dinitrophenol has no effect on it
(Ref. 1, p. 283)
  1. Lovastatin and mevastatin lower:
    1. Serum triglycerides
    2. Serum cholesterol
    3. Serum phospholipids
    4. All of the above
(Ref. 1, pp. 285-286)
  1. Lovastatin is a:
    1. Competitive inhibitor of acetyl CoA carboxylase
    2. Competitive inhibitor of HMG CoA synthetase
    3. Non-competitive inhibitor of HMG CoA reductase
    4. Competitive inhibitor of HMG CoA reductase (Ref. 2, p. 702)
  1. Abetalipoproteinaemia occurs due to a defect in the:
    1. Synthesis of apo B
    2. Loading of apo B with lipids
    3. Catabolism of apo B
    4. LDL receptors
(Ref. 1, p.272)
  1. All the following statements about Tangier disease are true except:
    1. It is a disorder of HDL metabolism
    2. It increases the risk of atherosclerosis
    3. Plasma triglycerides are increased in it
    4. Plasma HDL is increased in it
(Ref. 1, p.296)
108 C
109 D
110 C
111 B
112 D
113 B
114 D
138
  1. Genetic deficiency of lipoprotein lipase causes hyperlipoproteinaemia of following type:
    1. Type I
    2. Type IIa
    3. Type IIb
    4. Type V
(Ref. 1, p. 296)
  1. Chylomicrons are present in fasting blood samples in hyperlipoproteinaemia of following types:
    1. Types I and IIa
    2. Types IIa and IIb
    3. Types I and V
    4. Types IV and V
(Ref. 5, pp. 533-534)
  1. Glutathione is a constituent of:
    1. Leukotriene A4
    2. Thromboxane A1
    3. Leukotriene C4
    4. None of the above
(Ref. 1, pp. 256-257)
  1. Prostaglandins are inactivated by:
    1. 15-Hydroxyprostaglandin dehydrogenase
    2. Cyclo-oxygenase
    3. Lipo-oxygenase
    4. None of the above
(Ref. 1, p. 254)
  1. Aspirin and indomethacin inhibit:
    1. Phospholipase A1
    2. Phospholipase A2
    3. Cyclo-oxygenase
    4. Lipo-oxygenase
(Ref. 1, p. 254)
  1. Prostaglandins stimulate:
    1. Aggregation of platelets
    2. Lipolysis in adipose tissue
    3. Bronchodilatation
    4. Gastric acid secretion
(Ref. 5, p. 68)
  1. For extramitochondrial fatty acid synthesis, acetyl CoA may be obtained from:
    1. Citrate
    2. Isocitrate
    3. Oxaloacetate
    4. Succinate
(Ref. 1, pp. 231-234)
115 A
116 C
117 C
118 A
119 C
120 C
121 A
139
  1. Fluidity of membranes is increased by the following constituent:
    1. Polyunsaturated fatty acids
    2. Saturated fatty acids
    3. Integral proteins
    4. Cholesterol
(Ref. 1, p. 511)
  1. Transition temperature of membranes may be affected by the following constituent of membranes:
    1. Peripheral proteins
    2. Integral proteins
    3. Cholesterol
    4. Oligosaccharides
(Ref. 1, p. 511)
  1. Acetyl CoA formed from pyruvate can be used for the synthesis of all the following except:
    1. Glucose
    2. Fatty acids
    3. Cholesterol
    4. Steroid hormones
(Ref. 1, pp 233 285)
  1. The following can be used as a source of energy in extrahepatic tissues:
    1. Acetoacetate
    2. Acetone
    3. Both of the above
    4. Neither of the above
(Ref. 1, pp. 243-244)
  1. Anti-inflammatory corticosteroids inhibit:
    1. Phospholipase A1
    2. Synthesis of PGHS-2
    3. Cyclo-oxygenase
    4. Lipo-oxygenase
(Ref. 1, p. 254)
  1. Cyclo-oxygenase is involved in the synthesis of:
    1. Prostaglandins
    2. Thromboxanes
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 254)
  1. Leukotrienes cause:
    1. Increase in capillary permeability
    2. Aggregation of platelets
    3. Bronchodilatation
    4. None of the above (Ref. 5, p. 74)
122 A
123 C
124 A
125 A
126 B
127 C
128 A
140
  1. Prostaglandins decrease all of the following except:
    1. Gastric acid secretion
    2. Blood pressure
    3. Uterine contraction
    4. Platelet aggregation (Ref. 5, pp. 68-69)
  1. Hypocholesterolaemia can occur in:
    1. Hyperthyroidism
    2. Nephrotic syndrome
    3. Obstructive jaundice
    4. Diabetes mellitus (Ref. 5, p. 517)
  1. De novo synthesis and oxidation of fatty acids differ in the following respect:
    1. Synthesis occurs in cytosol and oxidation in mitochondria
    2. Synthesis is decreased and oxidation increased by insulin
    3. NADH is required in synthesis and FAD in oxidation
    4. Malonyl CoA is formed during oxidation but not during synthesis
(Ref. 1, pp. 237-238)
  1. Free fatty acids released from adipose tissue are transported in blood by:
    1. Albumin
    2. VLDL
    3. LDL
    4. HDL
(Ref. 1, p. 238)
  1. β-Galactosidase is deficient in:
    1. Fabry's disease
    2. Krabbe's disease
    3. Gaucher's disease
    4. Metachromatic leukodystrophy
(Ref. 1, p. 267)
  1. The enzyme deficient in metachromatic leukodystrophy is:
    1. Arylsulphatase A
    2. Hexosaminidase A
    3. Ceramidase
    4. Sphingomyelinase
(Ref. 1, p. 267)
129 C
130 A
131 A
132 A
133 B
134 A
141
  1. All the following statements about generalised gangliosidosis are true except:
    1. It results from deficiency of GM1-β-gangliosidase
    2. Breakdown of GM1, ganglioside is impaired
    3. GM2 ganglioside accumulates in liver and elsewhere
    4. It leads to mental retardation
(Ref. 1, p. 267)
  1. Hexosaminidase A is deficient in:
    1. Tay-Sachs disease
    2. Gaucher's disease
    3. Niemann-Pick disease
    4. Fabry's disease
(Ref. 1, p. 267)
  1. Mental retardation occurs in:
    1. Tay-Sachs disease
    2. Gaucher's disease
    3. Niemann-Pick disease
    4. All of the above
(Ref. 1, p. 267)
  1. The enzyme deficient in Fabry's disease is:
    1. α-Galactosidase
    2. β-Galactosidase
    3. α-Glucosidase
    4. β-Glucosidase
(Ref. 1, p. 267)
  1. Ceramidase is deficient in:
    1. Fabry's disease
    2. Farber's disease
    3. Krabbe's disease
    4. Tay-Sachs disease
(Ref. 1, p. 267)
  1. Ceramide is present in all of the following except:
    1. Plasmalogens
    2. Cerebrosides
    3. Sulphatides
    4. Sphingomyelin
(Ref. 1, pp. 263, 265)
  1. Fatty acids synthesised de novo in human beings generally:
    1. Have one double bond
    2. Are branched
    3. Have an even number of carbon atoms
    4. Have 18 carbon atoms
(Ref. 1, pp. 230-233)
135 C
136 A
137 D
138 A
139 B
140 A
141 C
142
  1. Fatty acids synthesised de novo in mammary glands:
    1. Are unbranched
    2. Are saturated
    3. May contain 8-12 carbon atoms
    4. All of the above
(Ref. 1, p. 233)
  1. The initial event in de novo synthesis of fatty acids is the transfer of:
    1. An acetyl group to -SH group of a cysteine residue
    2. A malonyl group to -SH group of a cysteine residue
    3. An acetyl group to -SH group of ACP
    4. A malonyl group to -SH group of ACP
(Ref. 1, p. 231)
  1. All the following statements about de novo synthesis of fatty acids in human beings are correct except:
    1. The source of carbon atoms is acetyl CoA
    2. The product is palmitoyl CoA
    3. NADPH is used as a reductant
    4. Two fatty acid molecules are synthesised simultaneously
(Ref. 1, pp. 230-233)
  1. De novo synthesis of fatty acids requires all the following vitamins (or their coenzymes) except:
    1. Niacin
    2. Pantothenic acid
    3. Folic acid
    4. Biotin
(Ref. 1, p. 230)
  1. Acetyl CoA carboxylase:
    1. Is a multienzyme protein
    2. Contains biotin
    3. Can exist in a dimeric or a polymeric form
    4. All of the above
(Ref. 1, pp. 230, 236)
  1. The initial event in carboxylation of acetyl CoA is:
    1. Formation of enzyme-biotin-ATP complex
    2. Carboxylation of biotin
    3. C Transfer of carboxyl group to ATP
    4. Transfer of carboxyl group to acetyl CoA
(Ref. 1, p. 230)
142 D
143 A
144 B
145 C
146 D
147 B
143
  1. All the following statements about acetyl CoA carboxylase are correct except:
    1. It is an allosteric enzyme
    2. Its allosteric activator is citrate
    3. Its allosteric inhibitor is long chain acyl CoA
    4. Allosteric activation involves conversion of polymeric form of the enzyme into dimeric form
(Ref. 1, p. 236)
  1. Insulin:
    1. Is an allosteric activator of acetyl CoA carboxylase
    2. Is an inducer of acetyl CoA carboxylase
    3. Causes phosphorylation of acetyl CoA carboxylase
    4. All of the above
(Ref. 1, p. 236)
  1. In de novo synthesis of fatty acids:
    1. A malonyl group is added to cysteine-SH in each cycle of reactions
    2. Each cycle adds three carbon atoms to the acyl group
    3. Thioesterase catalyses the last reaction in each cycle
    4. The priming carbon atom appears at the methyl end of the fatty acid
(Ref. 1, pp. 231-233)
  1. All the following statements about peroxisomes are correct except:
    1. Very long chain fatty acids are oxidised in peroxisomes
    2. Hydrogen peroxide is formed during oxidation of fatty acids in peroxisomes
    3. Carnitine palmitoyl transferase is required to transport fatty acids into peroxisomes
    4. They are congenitally absent in Zellweger's syndrome
(Ref. 1, pp. 240, 248)
  1. Peroxisomes participate in the synthesis of all of the following except:
    1. Cholesterol
    2. Bile acids
    3. Ether glycerophospholipids
    4. Very long chain fatty acids
(Ref. 1, p. 240)
148 D
149 B
150 D
151 C
152 D
144
  1. In Zellweger's syndrome:
    1. Transport of fatty acids into peroxisomes is impaired
    2. Very long chain fatty acids accumulate in peroxisomes
    3. Synthesis of bile acids is impaired
    4. Peroxisomes are absent in some tissues
(Ref. 1, p. 248)
  1. Human desaturase enzyme system:
    1. Is present in mitochondria
    2. Contains a cytochrome
    3. Acts only on 18-carbon fatty acids
    4. Introduces trans double bonds
(Ref. 1, p. 251)
  1. Deficiency of carnitine can impair:
    1. Uptake of long chain fatty acids by cells
    2. Uptake of very long chain fatty acids by peroxisomes
    3. Oxidation of long chain fatty acids in mitochondria
    4. All of the above
(Ref. 1, pp. 239-240)
  1. Hydrogen peroxide is formed during oxidation of fatty acids in:
    1. Peroxisomes
    2. Mitochondria
    3. Cytosol
    4. None of the above
(Ref. 1, p. 240)
  1. The following are present in outer mitochondrial membrane:
    1. Thiokinase (acyl CoA synthetase) and carnitine palmitoyl transferase I
    2. Thiokinase and carnitine palmitoyl transferase II
    3. Carnitine palmitoyl transferase I and carnitine palmitoyl transferase II
    4. Carnitine palmitoyl transferase II and carnitine acylcarnitine translocase
(Ref. 1, p. 239)
  1. The following are present in inner mitochondrial membrane:
    1. Thiokinase and carnitine palmitoyl transferase I
    2. Thiokinase and carnitine palmitoyl transferase II
    3. Carnitine palmitoyl transferase I and carnitine palmitoyl transferase II
    4. Carnitine palmitoyl transferase II and carnitine acylcarnitine translocase
(Ref. 1, p. 239)
153 C
154 B
155 C
156 A
157 A
158 D
145
  1. Carnitine acetyltransferase is present:
    1. In outer mitochondrial membrane
    2. In inner mitochondrial membrane
    3. Inside mitochondria
    4. None of the above
(Ref. 1, p.239)
  1. Sperms can obtain energy from:
    1. Acetylcarnitine
    2. Fructose
    3. Lactate
    4. All of the above
(Ref. 1, p.239)
  1. Acetone is formed from acetoacetate by:
    1. Acetoacetate dehydrogenase
    2. Acetoacetate carboxylase
    3. Acetoacetate decarboxylase
    4. Spontaneous decarboxylation
(Ref. 1, p.242)
  1. Two enzymes essential for ketogenesis are:
    1. HMG CoA synthetase and HMG CoA lyase
    2. HMG CoA synthetase and HMG CoA reductase
    3. HMG CoA reductase and HMG CoA lyase
    4. HMG CoA reductase and 3-hydroxybutyrate dehydrogenase
(Ref. 1, p.244)
  1. Normal concentration of ketone bodies in blood of well-fed men is:
    1. Less than 0.2 mmol / L
    2. 0.2 - 1 mmol / L
    3. 1 - 2 mmol / L
    4. 2 - 5 mmol / L
(Ref. 1, p. 243)
  1. Normal excretion of ketone bodies in urine of well-fed men is:
    1. Less than 1 mg / 24 hours
    2. B 1 -5 mg / 24 hours
    3. 5 - 10 mg / 24 hours
    4. 10-100 mg / 24 hours
(Ref. 1, p.243)
  1. Activation of acetoacetate requires:
    1. Malonyl CoA
    2. Succinyl CoA
    3. Acetyl CoA
    4. Propionyl CoA
(Ref. 1, p.245)
159 C
160 D
161 D
162 A
163 A
164 A
165 B
146
  1. Deficiency of carnitine can cause all the following except:
    1. Hypoglycaemia
    2. Lipid accumulation
    3. Muscular weakness
    4. Ketosis
(Ref. 1, p. 247)
  1. All the following statements about LDL receptors are true except:
    1. They are present in clathrin-coated pits in the cell membrane
    2. They transfer LDL inside the cell by receptor-mediated endocytosis
    3. They are present only in extrahepatic tissues
    4. They are down-regulated by cholesterol influx into the cell
(Ref. 1, pp. 290-291)
  1. All of the following act as ligands for receptors except:
    1. Apo A-I
    2. Apo B-100
    3. Apo C-II
    4. Apo E
(Ref. 1, p. 270)
  1. All the following statements about apo B-100 are correct except:
    1. It is synthesised in liver
    2. It is present in VLDL, IDL and LDL
    3. One molecule of apo B-100 is present per lipoprotein particle
    4. Its amino terminal region acts as the ligand for receptor
(Ref. 1, p. 274)
  1. All the following statements about apoprotein B-48 are correct except:
    1. It is encoded by the same gene that encodes apoprotein B-100
    2. It is 48% in size as compared to apoprotein B-100
    3. It is present in chylomicrons
    4. It is a ligand for chylomicron remnant receptor
(Ref. 1, p. 270)
166 D
167 C
168 C
169 D
170 D
147
  1. All the following statements about cholesterol synthesis are correct except:
    1. It is synthesised in animals only
    2. Liver and intestine synthesise significant amounts of cholesterol in man
    3. It can be synthesised in all nucleated cells
    4. Synthesis occurs partly in mitochondria and partly on microsomes
(Ref. 1, p. 285)
  1. The rate-limiting step in cholesterol synthesis is catalysed by:
    1. Thiolase
    2. HMG CoA synthetase
    3. HMG CoA reductase
    4. Mevalonate kinase
(Ref. 1, p. 285)
  1. An isoprenoid unit amongst the following is:
    1. Mevalonate pyrophosphate
    2. Isopentenyl pyrophosphate
    3. Geranyl pyrophosphate
    4. Farnesyl pyrophosphate
(Ref. 1, p. 286)
  1. NADPH is required in all the following reactions of cholesterol synthesis except:
    1. Conversion of HMG CoA into mevalonate
    2. Conversion of farnesyl pyrophosphate into squalene
    3. Conversion of squalene into squalene epoxide
    4. Conversion of squalene epoxide into lanosterol
(Ref. 1, pp. 286-288)
  1. Cholesterol synthesis is regulated by:
    1. Feedback inhibition
    2. Repression-derepression
    3. Covalent modification
    4. All of the above
(Ref. 1, p. 289)
  1. Esterification of cholesterol in the cells is catalysed by:
    1. Lecithin : cholesterol acyltransferase
    2. Acyl CoA : cholesterol acyltransferase
    3. Succinyl CoA : cholesterol acyltransferase
    4. Malonyl CoA : cholesterol acyltransferase
(Ref. 1, p. 290)
171 D
172 C
173 B
174 D
175 D
176 B
148
  1. Esterification of cholesterol in plasma is catalysed by:
    1. Lecithin : cholesterol acyltransferase
    2. Acyl CoA : cholesterol acyltransferase
    3. Succinyl CoA : cholesterol acyltransferase
    4. Malonyl CoA : cholesterol acyltransferase
(Ref. 1, p. 290)
  1. All the following statements about the synthesis of bile acids are correct except:
    1. Bile acids are formed from cholesterol in liver
    2. The rate - limiting step is catalysed by 12 α-hydroxylase
    3. The side chain attached to C17 is shortened
    4. Primary bile acids are cholic acid and chenodeoxycholic acid
(Ref. 1, pp. 292-293)
  1. All the following statements about the synthesis of bile acids are correct except:
    1. The rate-limiting step is catalysed by 7 α-hydroxylase
    2. The synthesis is decreased in vitamin C deficiency
    3. Three carbon atoms from the side chain are removed as propionyl CoA
    4. Deoxycholic acid and lithocholic acid are primary bile acids
(Ref. 1, pp. 292-293)
  1. All the following statements about lipoprotein (a) are correct except:
    1. It is also known as lipoprotein X
    2. It consists of 1 mol of LDL and 1 mol of Apo (a)
    3. Apo (a) shows structural homology to plasminogen
    4. Increased plasma level of lipoprotein (a) increases the risk of atherosclerosis
(Ref. 1, p. 296)
177 A
178 B
179 D
180 A

Metabolism of Nucleotides13

  1. Nucleotides required for the synthesis of nucleic acids can be obtained from:
    1. Dietary nucleic acids and nucleotides
    2. De novo synthesis
    3. Salvage of pre-existing bases and nucleosides
    4. De novo synthesis and salvage
(Ref. 1, pp. 386-388)
  1. In mammals, the major site for de novo synthesis of purine nucleotides is:
    1. Bone marrow
    2. Liver
    3. Brain
    4. Muscles
(Ref. 1, p. 390)
  1. The nitrogen atoms for de novo synthesis of purine nucleotides are provided by:
    1. Aspartate and glutamate
    2. Aspartate and glycine
    3. Aspartate, glutamine and glycine
    4. Aspartate, glutamate and glycine
(Ref. 1, p. 387)
  1. For de novo synthesis of purine nucleotides, glycine provides:
    1. One nitrogen atom
    2. One nitrogen and one carbon atom
    3. Two carbon atoms
    4. One nitrogen and two carbon atoms
(Ref. 1, p. 387)
1 D
2 B
3 C
4 D
150
  1. For de novo synthesis of purine nucleotides, aspartate provides:
    1. Nitrogen 1
    2. Nitrogen 3
    3. Nitrogen 7
    4. Nitrogen 9
(Ref. 1, p. 387)
  1. In the purine nucleus, carbon 6 is contributed by:
    1. Glycine
    2. CO2
    3. Aspartate
    4. Glutamine
(Ref. 1, p. 387)
  1. 5-Phosphoribosyl-1-pyrophosphate is required for the synthesis of:
    1. Purine nucleotides
    2. Pyrimidine nucleotides
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 387)
  1. Inosine monophosphate is an intermediate during de novo synthesis of:
    1. AMP and GMP
    2. CMP and UMP
    3. CMP and TMP
    4. All of the above
(Ref. 1, pp. 389, 393)
  1. Xanthosine monophosphate is an intermediate during de novo synthesis of:
    1. TMP
    2. CMP
    3. AMP
    4. GMP
(Ref. 1, pp. 389, 393)
  1. In the pathway of de novo synthesis of purine nucleotides, all the following are allosteric enzymes except:
    1. PRPP glutamyl amido transferase
    2. Adenylosuccinate synthetase
    3. IMP dehydrogenase
    4. Adenylosuccinase
(Ref. 1, p. 391)
  1. All the following enzymes are unique to purine nucleotide synthesis except:
    1. PRPP synthetase
    2. PRPP glutamyl amido transferase
    3. Adenylosuccinate synthetase
    4. IMP dehydrogenase
(Ref. 1, pp. 388-389)
5 A
6 B
7 C
8 A
9 D
10 D
11 A
151
  1. PRPP synthetase is allosterically inhibited by:
    1. AMP
    2. ADP
    3. GMP
    4. All of the above
(Ref. 1, p. 391)
  1. An allosteric inhibitor of PRPP glutamyl amido transferase is:
    1. AMP
    2. ADP
    3. GMP
    4. All of the above
(Ref. 1, p. 391)
  1. An allosteric inhibitor of adenylosuccinate synthetase is:
    1. AMP
    2. ADP
    3. GMP
    4. GDP
(Ref. 1, p. 391)
  1. An allosteric inhibitor of IMP dehydrogenase is:
    1. AMP
    2. ADP
    3. GMP
    4. GDP
(Ref. 1, p. 391)
  1. GMP is an allosteric inhibitor of all the following except:
    1. PRPP synthetase
    2. PRPP glutamyl amido transferase
    3. IMP dehydrogenase
    4. Adenylosuccinate synthetase
(Ref. 1, p. 391)
  1. AMP is an allosteric inhibitor of:
    1. PRPP synthetase
    2. Adenylosuccinate synthetase
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 391)
  1. The first reaction unique to purine nucleotide synthesis is catalysed by:
    1. PRPP synthetase
    2. PRPP glutamyl amido transferase
    3. Phosphoribosyl glycinamide synthetase
    4. Formyl transferase
(Ref. 1, p. 391)
12 D
13 C
14 A
15 C
16 D
17 C
18 B
152
  1. Free purine bases which can be salvaged are:
    1. Adenine and guanine
    2. Adenine and hypoxanthine
    3. Guanine and hypoxanthine
    4. Adenine, guanine and hypoxanthine
(Ref. 1, p. 390)
  1. The enzyme required for salvage of free purine bases is:
    1. Adenine phosphoribosyl transferase
    2. Hypoxanthine guanine phosphoribosyl transferase
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 390)
  1. Deoxycytidine kinase can salvage:
    1. Deoxycytidine
    2. Deoxyadenosine
    3. Deoxyguanosine
    4. All of the above
(Ref. 1, p. 390)
  1. Adenosine kinase can salvage:
    1. Adenosine
    2. Adenosine and deoxyadenosine
    3. Adenosine and guanosine
    4. Adenine and adenosine
(Ref. 1, p. 390)
  1. Salvage of purine bases is regulated by:
    1. Adenosine phosphoribosyl transferase
    2. Hypoxanthine guanine phosphoribosyl transferase
    3. Availability of PRPP
    4. None of the above
(Ref. 1, pp. 390-391)
  1. PRPP is used for all of the following except:
    1. De novo synthesis of purine nucleotides
    2. De novo synthesis of pyrimidine nucleotides
    3. Salvage of purine bases
    4. Salvage of pyrimidine bases
(Ref. 1, p. 387)
  1. The end product of purine catabolism in man is:
    1. Inosine
    2. Hypoxanthine
    3. Xanthine
    4. Uric acid
(Ref. 1, p. 395)
19 D
20 C
21 D
22 B
23 C
24 D
25 D
153
  1. The enzyme common to catabolism of all the purines is:
    1. Adenosine deaminase
    2. Purine nucleoside phosphorylase
    3. Guanase
    4. None of the above
(Ref. 1, p. 396)
  1. Uric acid is the end product of purine as well as protein catabolism in:
    1. Man
    2. Fish
    3. Birds
    4. None of the above
(Ref. 1, p. 387)
  1. Daily uric acid excretion in adult men is:
    1. 2-6 mg
    2. 20-40 mg
    3. 150-250 mg
    4. 400-600 mg
(Ref. 1, p. 395)
  1. Dietary purines are catabolised in:
    1. Liver
    2. Kidneys
    3. Intestinal mucosa
    4. All of the above
(Ref. 1, p. 386)
  1. All, except one, reactions of de novo synthesis of pyrimidine nucleotides occur in:
    1. Mitochondria
    2. Cytosol
    3. Peroxisomes
    4. Microsomes
(Ref. 1, p.392)
  1. All the following statements about carbamoyl phosphate synthetase II are correct except:
    1. It initiates de novo synthesis of pyrimidine nucleotides
    2. It is located in mitochondria
    3. Its substrates are glutamine, CO2 and ATP
    4. It is an allosteric enzyme
(Ref. 1, p. 392)
  1. The nitrogen atoms of pyrimidine nucleus are provided by:
    1. Glutamate
    2. Glutamate and aspartate
    3. Glutamine
    4. Glutamine and aspartate
(Ref. 1, p. 394)
26 B
27 C
28 D
29 C
30 B
31 B
32 D
154
  1. The carbon atoms of pyrimidine nucleus are provided by:
    1. Glycine and aspartate
    2. CO2 and aspartate
    3. CO2 and glutamate
    4. CO2 and glutamine
(Ref. 1, p. 393)
  1. Nitrogen at position 1 of pyrimidine nucleus comes from:
    1. Glutamine
    2. Glutamate
    3. Glycine
    4. Aspartate
(Ref. 1, p. 393)
  1. Nitrogen at position 3 of pyrimidine nucleus comes from:
    1. Glutamine
    2. Glutamate
    3. Glycine
    4. Aspartate
(Ref. 1, p. 393)
  1. The carbon atom at position 2 of pyrimidine nucleus is contributed by:
    1. CO2
    2. Glycine
    3. Aspartate
    4. Glutamine
(Ref. 1, p. 393)
  1. Aspartate contributes the following carbon atoms of the pyrimidine nucleus:
    1. C2 and C4
    2. C5 and C6
    3. C2, C4 and C6
    4. C4, C5 and C6
(Ref. 1, p. 393)
  1. The first pyrimidine nucleotide to be formed in de novo synthetic pathway is:
    1. UMP
    2. CMP
    3. CTP
    4. TMP
(Ref. 1, p. 393)
  1. Conversion of uridine diphosphate into deoxyuridine diphosphate requires all the following except:
    1. Ribonucleotide reductase
    2. Thioredoxin
    3. Tetrahydrobiopterin
    4. NADPH
(Ref. 1, pp. 392-393)
33 B
34 D
35 A
36 A
37 D
38 A
39 C
155
  1. Amethopterin and aminopterin decrease the synthesis of:
    1. TMP
    2. UMP
    3. CMP
    4. All of the above
(Ref. 2, p. 753)
  1. For synthesis of CTP from UTP, the amino group comes from:
    1. Amide group of asparagine
    2. Amide group of glutamine
    3. α-Amino group of glutamine
    4. α-Amino group of glutamate
(Ref. 2, p. 747)
  1. CTP synthetase forms CTP from:
    1. CDP and inorganic phosphate
    2. CDP and ATP
    3. UTP and glutamine
    4. UTP and glutamate
(Ref. 1, p. 393)
  1. For the synthesis of TMP from dUMP, a coenzyme is required which is:
    1. N10-Formyl tetrahydrofolate
    2. N5-Methyl tetrahydrofolate
    3. N5, N10-Methylene tetrahydrofolate
    4. N5-Formimino tetrahydrofolate
(Ref. 1, p. 393)
  1. All the enzymes required for de novo synthesis of pyrimidine nucleotides are cytosolic except:
    1. Carbamoyl phosphate synthetase
    2. Aspartate transcarbamoylase
    3. Dihydro-orotase
    4. Dihydro-orotate dehydrogenase
(Ref. 1, p. 392)
  1. During de novo synthesis of pyrimidine nucleotides, the first ring compound to be formed is:
    1. Carbamoyl aspartic acid
    2. Dihydro-orotic acid
    3. Orotic acid
    4. Orotidine monophosphate
(Ref. 1, p. 393)
40 A
41 B
42 C
43 C
44 D
45 B
156
  1. Tetrahydrofolate is required as a coenzyme for the synthesis of:
    1. UMP
    2. CMP
    3. TMP
    4. All of the above
(Ref. 1, p. 393)
  1. All the following statements about thioredoxin reductase are true except:
    1. It requires NADH as a coenzyme
    2. Its substrates are ADP, GDP, CDP and UDP
    3. It is activated by ATP
    4. It is inhibited by dADP
(Ref. 1, p. 392)
  1. De novo synthesis of pyrimidine nucleotides is regulated by:
    1. Carbamoyl phosphate synthetase
    2. Aspartate transcarbamoylase
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 394)
  1. Cytosolic carbamoyl phosphate synthetase is inhibited by:
    1. UTP
    2. CTP
    3. PRPP
    4. TMP
(Ref. 1, p. 394)
  1. Cytosolic carbamoyl phosphate synthetase is activated by:
    1. Glutamine
    2. PRPP
    3. ATP
    4. Aspartate
(Ref. 1, p. 394)
  1. Aspartate transcarbamoylase is inhibited by:
    1. CTP
    2. PRPP
    3. ATP
    4. TMP
(Ref. 1, p. 394)
  1. The following cannot be salvaged in human beings:
    1. Cytidine
    2. Deoxycytidine
    3. Cytosine
    4. Thymidine
(Ref. 1, p. 394)
  1. β-Aminoisobutyrate is formed from catabolism of:
    1. Cytosine
    2. Uracil
    3. Thymine
    4. Xanthine
(Ref. 1, p. 399)
46 C
47 A
48 C
49 A
50 B
51 A
52 C
53 C
157
  1. Free ammonia is liberated during the catabolism of:
    1. Cytosine
    2. Uracil
    3. Thymine
    4. All of the above
(Ref. 1, p. 399)
  1. β-Alanine is formed from catabolism of:
    1. Thymine
    2. Thymine and cytosine
    3. Thymine and uracil
    4. Cytosine and uracil
(Ref. 1, p. 399)
  1. The following coenzyme is required for catabolism of pyrimidine bases:
    1. NADH
    2. NADPH
    3. FADH2
    4. None of the above
(Ref. 1, p. 399)
  1. Inheritance of primary gout is:
    1. Autosomal recessive
    2. Autosomal dominant
    3. X-linked recessive
    4. X-linked dominant
(Ref. 1, p. 397)
  1. The following abnormality in PRPP synthetase can cause primary gout:
    1. High Vmax
    2. Low Km
    3. Resistance to allosteric inhibition
    4. Any of the above
(Ref. 1, p. 397)
  1. All the following statements about primary gout are true except:
    1. Its inheritance is X-linked recessive
    2. It can be due to increased activity of PRPP synthetase
    3. It can be due to increased activity of hypoxanthine guanine phosphoribosyl transferase
    4. De novo synthesis of purines is increased in it
(Ref. 1, p. 397)
  1. All the following statements about uric acid are true except:
    1. It is a catabolite of purines
    2. It is excreted by the kidneys
    3. It is undissociated at pH above 5.8
    4. It is less soluble than sodium urate
(Ref. 1, p. 395)
54 D
55 D
56 B
57 C
58 D
59 C
60 C
158
  1. In partial deficiency of hypoxanthine guanine phosphoribosyl transferase:
    1. De novo synthesis of purine nucleotides is increased
    2. Salvage of pyrimidines is decreased
    3. Salvage of purines is increased
    4. Synthesis of uric acid is decreased
(Ref. 1, p. 397)
  1. All the following statements about uric acid are true except:
    1. It can be formed from allantoin
    2. Formation of uric acid stones in kidneys can be decreased by alkalinisation of urine
    3. Uric acid begins to dissociate at pH above 5.8
    4. It is present in plasma mainly as monosodium urate
(Ref. 1, p. 395)
  1. All the following statements about primary gout are true except:
    1. Uric acid stones may be formed in kidneys
    2. Arthritis of small joints occurs commonly
    3. Urinary excretion of uric acid is decreased
    4. It occurs predominantly in males
(Ref. 6, pp. 271-272)
  1. All the following statements about allopurinol are true except:
    1. It is a structural analogue of uric acid
    2. It can prevent uric acid stones in the kidneys
    3. It increases the urinary excretion of xanthine and hypoxanthine
    4. It is a competitive inhibitor of xanthine oxidase
(Ref. 2, p. 757)
  1. Orotic aciduria can be controlled by:
    1. Oral administration of orotic acid
    2. Decreasing the dietary intake of orotic acid
    3. Decreasing the dietary intake of pyrimidines
    4. Oral administration of uridine
(Ref. 1, p. 398)
61 A
62 A
63 C
64 A
65 D
159
  1. All the following occur in orotic aciduria except:
    1. Increased synthesis of pyrimidine nucleotides
    2. Increased excretion of orotic acid in urine
    3. Decreased synthesis of cytidine triphosphate
    4. Retardation of growth
(Ref. 6, p. 274)
  1. Inherited deficiency of adenosine deaminase causes:
    1. Hyperuricaemia and gout
    2. Mental retardation
    3. Immunodeficiency
    4. Dwarfism
(Ref. 1, p. 398)
  1. Complete absence of hypoxanthine guanine phosphoribosyl transferase causes:
    1. Primary gout
    2. Immunodeficiency
    3. Uric acid stones
    4. Lesch-Nyhan syndrome
(Ref. 1, p. 397)
  1. Increased urinary excretion of orotic acid can occur in deficiency of:
    1. Orotate phosphoribosyl transferase
    2. OMP decarboxylase
    3. Mitochondrial ornithine transcarbamoylase
    4. Any of the above
(Ref. 1, p. 398)
  1. All of the following can occur in Lesch-Nyhan syndrome except:
    1. Gouty arthritis
    2. Uric acid stones
    3. Retarded growth
    4. Self-mutilating behaviour
(Ref. 2, p. 758)
  1. Inherited deficiency of purine nucleoside phosphorylase causes:
    1. Dwarfism
    2. Mental retardation
    3. Immunodeficiency
    4. Gout
(Ref. 1, p. 398)
  1. Deoxyribonucleotides are formed by reduction of:
    1. Ribonucleosides
    2. Ribonucleoside monophosphates
    3. Ribonucleoside diphosphates
    4. Ribonucleoside triphosphates
(Ref. 1, p. 392)
66 A
67 C
68 D
69 D
70 C
71 C
72 C
160
  1. An alternate substrate for orotate phosphoribosyl transferase is:
    1. Allopurinol
    2. Xanthine
    3. Hypoxanthine
    4. Adenine
(Ref. 1, p. 398)
  1. Mammals other than higher primates do not suffer from gout because they:
    1. Lack xanthine oxidase
    2. Lack adenosine deaminase
    3. Lack purine nucleoside phosphorylase
    4. Possess uricase
(Ref. 1, p. 395)
  1. Hypouricaemia can occur in:
    1. Xanthine oxidase deficiency
    2. Psoriasis
    3. Leukaemia
    4. None of the above
(Ref. 1, p. 398)
  1. 5-Phosphoribosyl-1-pyrophosphate is required for all of the following except:
    1. De novo synthesis of purine nucleotides
    2. De novo synthesis of pyrimidine nucleotides
    3. Salvage of adenine
    4. Salvage of cytosine
(Ref. 1, pp. 387, 390, 394)
  1. An anti-cancer drug that acts by inhibiting nucleotide synthesis is:
    1. Allopurinol
    2. Methotrexate
    3. α-Amanitin
    4. Azathioprine
(Ref. 1, pp. 383, 394)
  1. Phosphoribosyl transferases:
    1. Use PRPP as one of the substrates
    2. Transfer ribose-5-phosphate to nitrogenous bases
    3. Are involved in salvage of purines
    4. All of the above
(Ref. 1, p.390)
73 A
74 D
75 A
76 D
77 B
78 D
161
  1. A superactive PRPP synthetase can cause:
    1. Gout
    2. Lesch-Nyhan syndrome
    3. Immunodeficiency
    4. None of the above
(Ref. 1, p.397)
  1. Uric acid is:
    1. Formed from xanthine by a metalloflavoprotein enzyme
    2. An allosteric inhibitor of xanthine oxidase
    3. Excreted in bile
    4. A metabolite of purines and pyrimidines
(Ref. 1, pp. 131, 395, 398)
  1. Severe combined immunodeficiency disease (SCID) results from deficiency of:
    1. Adenosine kinase
    2. Adenosine deaminase
    3. Adenine phosphoribosyl transferase
    4. HGPRT
(Ref. 1, p.398)
  1. dUMP is converted into TMP by:
    1. Methylation
    2. Carboxylation
    3. Deamination
    4. Decarboxylation
(Ref. 1, p.393)
  1. Thioredoxin reductase is involved in the synthesis of:
    1. Deoxynucleoside monophosphates from nucleoside monophosphates
    2. Deoxynucleoside diphosphates from nucleoside diphosphates
    3. Deoxynucleoside triphosphates from nucleoside triphosphates
    4. All of the above
(Ref. 1, pp. 391-392)
  1. Glutamine is required for de novo synthesis of:
    1. Purine nucleotides
    2. Pyrimidine nucleotides
    3. Both of the above
    4. Neither of the above
(Ref. 1, pp. 387, 393)
79 A
80 A
81 B
82 A
83 B
84 C
162
  1. All the following statements about adenine and guanine nucleotides are correct except:
    1. Their de novo synthesis occurs from a common intermediate
    2. They are salvaged from free bases by a common enzyme
    3. They are catabolised to a common end product
    4. They occur in DNA as well as RNA
(Ref. 1,pp.389, 395, 402, 406)
  1. Purine nucleotides are synthesised de novo in human beings from:
    1. Hydrolysis of DNA
    2. Hydrolysis of RNA
    3. Amphibolic intermediates
    4. All of the above
(Ref. 1, p.386)
  1. Purine nucleotides can be formed by:
    1. De novo synthesis
    2. Phosphoribosylation of purine bases
    3. Phosphorylation of purine nucleosides
    4. All of the above
(Ref. 1, p.387)
  1. Immunodeficiency can be caused by deficiency of:
    1. Adenosine deaminase
    2. Purine nucleoside phosphorylase
    3. Both of the above
    4. Neither of the above
(Ref. 1, p.397)
  1. Deficiency of purine nucleoside phosphorylase:
    1. Is an X-linked inherited disease
    2. Causes immunodeficiency
    3. Affects both T cells and B cells
    4. Causes hyperuricaemia
(Ref. 1, p.397)
  1. Renal lithiasis (stone formation) can occur in all the following except:
    1. Lesch-Nyhan syndrome
    2. Adenosine phosphoribosyl transferase deficiency
    3. Xanthine oxidase deficiency
    4. Adenosine deaminase deficiency
(Ref. 1, pp. 397-398)
85 B
86 C
87 D
88 C
89 B
90 D
163
  1. Hypouricaemia can occur in:
    1. Purine nucleoside phosphorylase deficiency
    2. Xanthine oxidase deficiency
    3. Both of the above
    4. Neither of the above
(Ref. 1, p.397)
  1. Hyperuricaemia can occur due to all the following except:
    1. Superactive PRPP synthetase
    2. HGPRT deficiency
    3. Glucose-6-phosphatase deficiency
    4. Uricase deficiency
(Ref. 1, pp. 397-398)
  1. A pyrimidine nucleoside which is not catabolised further is:
    1. Thymidine
    2. Cytidine
    3. Uridine
    4. Pseudouridine
(Ref. 1, pp. 398-399)
  1. Salvage of purines and their nucleosides is the major source of purine nucleotides in:
    1. Brain
    2. Erythrocytes
    3. Polymorphonuclear leukocytes
    4. All of the above
(Ref. 1, p.390)
  1. All the following statements about hypoxanthine - guanine phosphoribosyl transferase are correct except:
    1. It is a salvage enzyme
    2. It forms IMP and GMP
    3. It is superactive in gout
    4. It is absent in Lesch-Nyhan syndrome
(Ref. 1, pp. 390, 397)
  1. Deficiency of orotidylate (OMP) decarboxylase can cause:
    1. Retardation of growth
    2. Immunodeficiency
    3. Megaloblastic anaemia
    4. All of the above
(Ref. 1, p.400)
91 C
92 D
93 D
94 D
95 C
96 C
164
  1. Deficiency of orotate phosphoribosyl transferase and orotidylate decarboxylase can cause:
    1. Retardation of growth
    2. Immunodeficiency
    3. Megaloblastic anaemia
    4. All of the above
(Ref. 1, p.400)
  1. Urinary excretion of orotic acid may be increased in deficiency of:
    1. Orotate phosphoribosyl transferase
    2. Orotidylate decarboxylase
    3. Ornithine transcarbamoylase
    4. All of the above
(Ref. 1, p.400)
  1. Deficiency of hepatic mitochondrial ornithine transcarbamoylase causes all the following except:
    1. Decreased utilisation of carbamoyl phosphate
    2. Exit of carbamoyl phosphate to cytosol
    3. Increased synthesis of pyrimidine nucleotides
    4. Megaloblastic anaemia
(Ref. 1, pp. 398, 400)
  1. Immunodeficiency can occur in all the following except:
    1. Orotic aciduria, type I
    2. Orotic aciduria, type II
    3. Adenosine deaminase deficiency
    4. Purine nucleoside phosphorylase deficiency
(Ref. 1, p.398, 400)
97 D
98 D
98 D
100 B

Metabolism of Nucleic Acids14

  1. Synthesis of DNA is also known as:
    1. Duplication
    2. Replication
    3. Transcription
    4. Translation
(Ref. 1, p. 405)
  1. Replication of DNA is:
    1. Conservative
    2. Semi-conservative
    3. Non-conservative
    4. None of the above
(Ref. 1, p. 405)
  1. Direction of DNA synthesis is:
    1. 5' → 3'
    2. 3' → 5'
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 424)
  1. Formation of RNA primer:
    1. Precedes replication
    2. Follows replication
    3. Precedes transcription
    4. Follows transcription
(Ref. 1, p. 424)
  1. Okazaki pieces are made up of:
    1. RNA
    2. DNA
    3. RNA and DNA
    4. RNA and proteins
(Ref. 1, p. 424)
  1. Okazaki pieces are formed during the synthesis of:
    1. mRNA
    2. tRNA
    3. rRNA
    4. DNA
(Ref. 1, p. 424)
1 B
2 B
3 A
4 A
5 C
6 D
166
  1. After formation of replication fork:
    1. Both the new strands are synthesised discontinuously
    2. One strand is synthesised continuously and the other discontinuously
    3. Both the new strands are synthesised continuously
    4. RNA primer is required only for the synthesis of one new strand
(Ref. 2, pp. 808-809)
  1. An Okazaki fragment contains about:
    1. 10 Nucleotides
    2. 100 Nucleotides
    3. 1,000 Nucleotides
    4. 10,000 Nucleotides
(Ref. 2, p. 804)
  1. RNA primer is formed by the enzyme:
    1. Ribonuclease
    2. Primase
    3. DNA polymerase I
    4. DNA polymerase III
(Ref. 1, p. 423)
  1. In RNA, the complementary base of adenine is:
    1. Cytosine
    2. Guanine
    3. Thymine
    4. Uracil
(Ref. 1, p. 408)
  1. During eukaryotic replication, the template DNA is unwound:
    1. At one of the ends
    2. At both the ends
    3. At multiple sites
    4. Nowhere
(Ref. 1, p. 427)
  1. During replication, unwinding of double helix is initiated by:
    1. dnaA protein
    2. dnaB protein
    3. dnaC protein
    4. rep protein
(Ref. 1, p. 423)
  1. For unwinding of double-helical DNA:
    1. Energy is provided by ATP
    2. Energy is provided by GTP
    3. Energy can be provided by either ATP or GTP
    4. No energy is required
(Ref. 2, p. 805)
7 B
8 C
9 B
10 D
11 C
12 B
13 A
167
  1. Helicase and dnaB protein cause:
    1. Rewinding of DNA and require ATP as a source of energy
    2. Rewinding of DNA but do not require any source of energy
    3. Unwinding of DNA and require ATP as a source of energy
    4. Unwinding of DNA but do not require any source of energy
(Ref. 2, pp. 805, 808)
  1. The unwound strands of DNA are held apart by:
    1. Single strand binding protein
    2. Double strand binding protein
    3. Rep protein
    4. dnaA protein
(Ref. 1, p. 423)
  1. Deoxyribonucleotides are added to RNA primer by:
    1. DNA polymerase I
    2. DNA polymerase II
    3. DNA polymerase III holoenzyme
    4. All of the above
(Ref. 1, p. 424)
  1. Ribonucleotides of RNA primer are replaced by deoxyribonucleotides by the enzyme:
    1. DNA polymerase I
    2. DNA polymerase II
    3. DNA polymerase III holoenzyme
    4. All of the above
(Ref. 2, p. 808)
  1. DNA fragments are sealed by:
    1. DNA polymerase II
    2. DNA ligase
    3. DNA gyrase
    4. DNA topoisomerase II
(Ref. 1, p. 426)
  1. Negative supercoils are introduced in DNA by:
    1. Helicase
    2. DNA ligase
    3. DNA gyrase
    4. DNA polymerase III holoenzyme
(Ref. 2, p. 799)
14 C
15 A
16 C
17 A
18 B
19 C
168
  1. Reverse transcriptase activity is present in the euliaryotic:
    1. DNA polymerase α
    2. DNA polymerase γ
    3. Telomerase
    4. DNA polymerase II
(Ref. 2, pp. 806-807)
  1. DNA polymerase III holoenzyme possesses:
    1. Polymerase activity
    2. 3' → 5' Exonuclease activity
    3. 5' → 3' Exonuclease and polymerase activities
    4. 3' → 5' Exonuclease and polymerase activities
(Ref. 2, pp. 806-807)
  1. DNA polymerase I possesses:
    1. Polymerase activity
    2. 3' → 5' Exonuclease activity
    3. 5' → 3' Exonuclease activity
    4. All of the above
(Ref. 2, p. 802)
  1. 3' → 5' Exonuclease activity of DNA polymerase I:
    1. Removes ribonucleotides
    2. Adds deoxyribonucleotides
    3. Corrects errors in replication
    4. Hydrolyses DNA into mononucleotides
(Ref. 2, p. 800)
  1. All the following statements about RNA-dependent DNA polymerase are true except:
    1. It synthesises DNA using RNA as a template
    2. It is also known as reverse transcriptase
    3. It synthesises DNA in 5' → 3' direction
    4. It is present in all the viruses
(Ref. 2, pp. 834-835)
  1. Reverse transcriptase catalyses:
    1. Synthesis of RNA
    2. Breakdown of RNA
    3. Synthesis of DNA
    4. Breakdown of DNA
(Ref. 2, p. 985)
20 C
21 D
22 D
23 C
24 D
25 C
169
  1. dna A protein can bind only to:
    1. Positively supercoiled DNA
    2. Negatively supercoiled DNA
    3. Neither of the above
    4. h of the above
(Ref. 2, p. 805)
  1. DNA topoisomerase I of E.coli catalyses:
    1. Relaxation of negatively supercoiled DNA
    2. Relaxation of positively supercoiled DNA
    3. Conversion of negatively supercoiled DNA into positively supercoiled DNA
    4. Conversion of double helix into supercoiled DNA
(Ref. 2, p. 797)
  1. In mammalian cell cycle, synthesis of DNA occurs during:
    1. S phase
    2. G1 phase
    3. Mitotic phase
    4. G2 phase
(Ref. 1, p. 428)
  1. Melting temperature of DNA is the temperature at which:
    1. Solid DNA becomes liquid
    2. DNA is hydrolysed into nucleotides
    3. DNA changes from double helix into supercoiled DNA
    4. Half of the helical structure of DNA is lost
(Ref. 2, pp. 84-86)
  1. Melting temperature of DNA is increased by its:
    1. A and T content
    2. G and C content
    3. Sugar content
    4. Phosphate content
(Ref. 1, p. 404)
  1. Buoyant density of DNA is increased by its:
    1. A and T content
    2. G and C content
    3. Sugar content
    4. None of the above
(Ref. 3, p. 810)
  1. Relative proportions of G and C versus A and T in DNA can be determined by its:
    1. Melting temperature
    2. Buoyant density
    3. Both of the above
    4. Neither of the above
(Ref. 3, p. 810)
26 B
27 A
28 A
29 D
30 B
31 B
32 C
170
  1. Some DNA is present in mitochondria of:
    1. Prokaryotes
    2. Eukaryotes
    3. Both of the above
    4. Neither of the above
(Ref. 2, pp. 988-989)
  1. Satellite DNA contains:
    1. Highly repetitive sequences
    2. Moderately repetitive sequences
    3. Non-repetitive sequences
    4. DNA-RNA hybrids
(Ref. 2, pp. 991-992)
  1. Synthesis of RNA from a DNA template is known as:
    1. Replication
    2. Translation
    3. Transcription
    4. Mutation
(Ref. 1, p. 435)
  1. Direction of RNA synthesis is:
    1. 5' → 3'
    2. 3' → 5'
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 435)
  1. Prokaryotic DNA-dependent RNA polymerase is a:
    1. Monomer
    2. Dimer
    3. Trimer
    4. Tetramer
(Ref. 1, p. 436)
  1. DNA-dependent RNA polymerase requires the following for its catalytic activity:
    1. Mg ++
    2. M++
    3. Either of the above
    4. Neither of the above
(Ref. 2, p. 100)
  1. The initiation site for transcription is recognised by:
    1. α-Subunit of DNA-dependent RNA polymerase
    2. β-Subunit of DNA-dependent RNA polymerase
    3. Sigma factor
    4. Rho factor
(Ref. 2, p. 842)
  1. The termination site for transcription is recognised by:
    1. α-Subunit of DNA-dependent RNA polymerase
    2. β-Subunit of DNA-dependent RNA polymerase
    3. Sigma factor
    4. Rho factor
(Ref. 1, p. 438)
33 B
34 A
35 C
36 A
37 D
38 C
39 C
40 D
171
  1. Mammalian RNA polymerase I synthesises:
    1. mRNA
    2. rRNA
    3. tRNA
    4. hnRNA
(Ref. 2, p. 853)
  1. Mammalian RNA polymerase III synthesises:
    1. rRNA
    2. mRNA
    3. tRNA
    4. hnRNA
(Ref. 2, p. 853)
  1. In mammals, synthesis of mRNA is catalysed by:
    1. DRNA polymerase I
    2. RNA polymerase II
    3. RNA polymerase III
    4. RNA polymerase IV
(Ref. 2, p. 853)
  1. Heterogeneous nuclear RNA is the precursor of:
    1. mRNA
    2. rRNA
    3. tRNA
    4. None of the above
(Ref. 1, p. 408)
  1. Post-transcriptional modification of hnRNA involves all of the following except:
    1. Addition of 7-methylguanosine triphosphate cap
    2. Addition of polyadenylate tail
    3. Insertion of nucleotides
    4. Deletion of introns
(Ref. 1, pp. 448, 449)
  1. Newly synthesised tRNA undergoes post-transcriptional modifications which include all the following except:
    1. Reduction in size
    2. Methylation of some bases
    3. Formation of pseudouridine
    4. Addition of C-C-A terminus at 5'-end
(Ref. 1, p. 450)
  1. Post-transcriptional modification does not occur in:
    1. Eukaryotic tRNA
    2. Prokaryotic tRNA
    3. Eukaryotic hnRNA
    4. Prokaryotic mRNA
(Ref. 1, p. 445)
41 B
42 C
43 B
44 A
45 C
46 D
47 D
172
  1. A consensus sequence on DNA, called TATA box, is the site for attachment of:
    1. RNA-dependent DNA polymerase
    2. DNA-dependent RNA polymerase
    3. DNA-dependent DNA polymerase
    4. DNA topoisomerase II
(Ref. 1, p. 439)
  1. Polyadenylate tail is not present in mRNA synthesising:
    1. Globin
    2. Histone
    3. Apoferritin
    4. Growth hormone
(Ref. 1, p. 448)
  1. Introns are present in DNA of:
    1. Viruses
    2. Bacteria
    3. Man
    4. All of the above
(Ref. 1, p. 445)
  1. A mammalian DNA polymerase among the following is:
    1. DNA polymerase α
    2. DNA polymerase I
    3. DNA polymerase II
    4. DNA polymerase IV
(Ref. 2, p. 983)
  1. Mammalian DNA polymerase γ is located in:
    1. Nucleus
    2. Nucleolus
    3. Mitochondria
    4. Cytosol
(Ref. 2, p. 983)
  1. Replication of nuclear DNA in mammals is catalysed by:
    1. DNA polymerase α
    2. DNA polymerase β
    3. DNA polymerase γ
    4. DNA polymerase III
(Ref. 2, p. 983)
  1. Primase activity is present in:
    1. DNA polymerase II
    2. DNA polymerase α
    3. DNA polymerase β
    4. DNA polymerase δ
(Ref. 2, p. 983)
  1. The mammalian DNA polymerase involved in error correction is:
    1. DNA polymerase α
    2. DNA polymerase β
    3. DNA polymerase γ
    4. DNA polymerase δ
(Ref. 2, p. 983)
48 B
49 B
50 C
51 A
52 C
53 A
54 B
55 B
173
  1. Novobiocin inhibits the synthesis of:
    1. DNA
    2. mRNA
    3. tRNA
    4. rRNA
(Ref. 2, p. 799)
  1. Ciprofloxacin inhibits the synthesis of:
    1. DNA
    2. mRNA
    3. tRNA
    4. rRNA
(Ref. 2, p. 799)
  1. Ciprofloxacin inhibits:
    1. DNA topoisomerase II
    2. DNA polymerase I
    3. DNA polymerase III
    4. DNA gyrase
(Ref. 2, p. 799)
  1. Rifampicin inhibits:
    1. Unwinding of DNA
    2. Initiation of replication
    3. Initiation of translation
    4. Initiation of transcription
(Ref. 2, p. 851)
  1. Actinomycin D binds to:
    1. Double-stranded DNA
    2. Single-stranded DNA
    3. Single-stranded RNA
    4. DNA-RNA hybrid
(Ref. 2, p. 851)
  1. DNA contains some 4-6 bp palindromic sequences which:
    1. Mark the site for the formation of replication forks
    2. Direct DNA polymerase to turn back to replicate the other strand
    3. Are recognised by restriction enzymes
    4. Are found only in bacterial DNA
(Ref. 2, p. 120)
  1. Introns in genes:
    1. Encode the amino acids which are removed during post-translational modification
    2. Encode signal sequences which are removed before secretion of the proteins
    3. Are the non-coding sequences which are not translated
    4. Are the sequences that intervene between two genes
(Ref. 1, p. 445)
56 A
57 A
58 D
59 D
60 A
61 C
62 C
174
  1. All the following statements about post-transcriptional processing of tRNA are true except:
    1. Introns of some tRNA precursors are removed
    2. CCA is added at 3' end
    3. 7-Methylguanosine triphosphate cap is added at 5' end
    4. Some bases are methylated
(Ref. 1, p. 450)
  1. α-Amanitin inhibits:
    1. DNA polymerase II of prokaryotes
    2. DNA polymerase α of eukaryotes
    3. RNA polymerase II of eukaryotes
    4. RNA-dependent DNA polymerase
(Ref. 2, p. 853)
  1. Ciprofloxacin inhibits the synthesis of:
    1. DNA in prokaryotes
    2. DNA in prokaryotes and eukaryotes
    3. RNA in prokaryotes
    4. RNA in prokaryotes and eukaryotes
(Ref. 2, p. 799)
  1. All the following statements about bacterial promoters are true except:
    1. They are smaller than eukaryotic promoters
    2. They have two consensus sequences upstream from the transcription start site
    3. TATA box is the site for attachment of RNA polymerase
    4. TATA box has a high melting temperature
(Ref. 1, pp. 439-440)
  1. All the following statements about eukaryotic promoters are true except:
    1. They may be located upstream or downstream from the structural gene
    2. They have two consensus sequences
    3. One consensus sequence binds RNA polymerase
    4. Mutations in promoter region can decrease the efficiency of transcription of the structural gene
(Ref. 1, pp. 439-440)
63 C
64 C
65 A
66 D
67 A
175
  1. In Sanger's method of DNA sequence determination, DNA synthesis is stopped by using:
    1. 1', 2'-Dideoxyribonucleoside triphosphates
    2. 2', 3'-Dideoxyribonucleoside triphosphates
    3. 2', 4'-Dideoxyribonucleoside triphosphates
    4. 2', 5'-Dideoxyribonucleoside triphosphates
(Ref. 2, p. 123)
  1. tRNA genes have:
    1. Upstream promoters
    2. Downstream promoters
    3. Intragenic promoters
    4. No promoters
(Ref. 1, p. 445)
  1. All the following statements about rRNA are true except:
    1. It is synthesised as a large precursor
    2. It is processed in the nucleolus
    3. It has no codons or anticodons
    4. Genes for rRNA are present in single copies
(Ref. 1, p. 447)
  1. Melting temperature of DNA is affected by:
    1. Its base composition
    2. Concentration of monovalent cations in the solution
    3. Formamide
    4. All of the above
(Ref. 1, p. 404)
  1. In DNA, G – C bonding is stronger than A – T bonding because:
    1. Three hydrogen bonds are present between G and C as opposed to two between A and T
    2. Bonding between G and C is covalent while that between A and T is non-covalent
    3. G and C do not have methyl groups
    4. The glycosidic bond in G and C nucleosides has a syn conformation
(Ref. 1, pp. 402-404)
  1. Circular double-stranded DNA:
    1. Has no free 5' and 3' ends
    2. Has no polarity (direction)
    3. Cannot be supercoiled
    4. All of the above
(Ref. 1, p. 405)
68 B
69 C
70 D
71 D
72 A
73 A
176
  1. All the following statements about topoisomerases are true except:
    1. They catalyse topological changes in DNA
    2. They can introduce or relax supercoils in DNA
    3. They can seal nicks in DNA
    4. They are found only in prokaryotes
(Ref. 1, pp. 405, 427)
  1. Chromatin contains:
    1. DNA and histones in roughly equal amounts
    2. A small amount of non-histone proteins
    3. A small amount of RNA
    4. All of the above
(Ref. 1, p. 412)
  1. Nuclear histones:
    1. Are basic proteins
    2. Form nucleosomes in which DNA is wrapped around a histone octamer
    3. Protect DNA from hydrolysis by nucleases
    4. All of the above
(Ref. 1, pp. 412-413)
  1. Transcriptionally inactive chromatin is:
    1. Called euchromatin
    2. Densely packed during interphase
    3. Replicated earlier in the mammalian cell cycle
    4. Found only in X chromosomes
(Ref. 1, pp. 414-415)
  1. Cyclins:
    1. Are circular DNA double helices
    2. Are circular polypeptides
    3. Are proteins that regulate cell cycle
    4. Can undergo phosphorylation and dephosphorylation
(Ref. 1, p. 429)
  1. The correct sequence of different phases of mammalian cell cycle is:
    1. Mitotic phase, G1 phase, S phase and G2 phase
    2. S phase, G1 phase, mitotic phase and G2 phase
    3. S phase, mitotic phase, G1 phase and G2 phase
    4. Mitotic phase, S phase, G1 phase and G2 phase
(Ref. 1, p. 429)
74 D
75 D
76 D
77 B
78 C
79 A
177
  1. All the following statements about cyclins are correct except:
    1. They are cyclic nucleotides
    2. Their concentrations vary in different phases of cell cycle
    3. They regulate the progression of cell cycle from one phase to the next
    4. They activate cyclin-dependent protein kinases
(Ref. 1, p. 428)
  1. An endonuclease hydrolyses phosphodiester bonds:
    1. At the 5'-end
    2. At the 3'-end
    3. In the interior of a nucleic acid
    4. All of the above
(Ref. 1, p. 489)
  1. An exonuclease hydrolyses phosphodiester bonds:
    1. Of exogenous nucleic acids
    2. Either at 5'-end or at 3'-end
    3. At both the ends
    4. Present in palindromic sequences
(Ref. 1, p. 489)
  1. A glycosylase is required in:
    1. Mismatch repair of DNA
    2. Base excision repair of DNA
    3. Nucleotide excision repair of DNA
    4. None of the above
(Ref. 1, pp. 430-432)
  1. GATC endonuclease is involved in:
    1. Mismatch repair of DNA
    2. Base excision repair of DNA
    3. Nucleotide excision repair of DNA
    4. All of the above
(Ref. 1, pp. 430-432)
  1. DNA ligase is required in:
    1. Mismatch repair of DNA
    2. Base excision repair of DNA
    3. Nucleotide excision repair of DNA
    4. All of the above
(Ref. 1, pp. 430-432)
80 A
81 C
82 B
83 B
84 A
85 D
178
  1. Mismatch repair of DNA:
    1. Occurs only in eukaryotes
    2. Occurs after the addition of every nucleotide during replication
    3. Occurs after replication
    4. Involves removal of methylated adenine bases
(Ref. 1, pp. 430-431)
  1. Both the strands of DNA act as templates in:
    1. Mismatch repair
    2. Base excision repair
    3. Nucleotide excision repair
    4. None of the above
(Ref. 1, pp. 430-432)
  1. Replication of DNA is:
    1. Semi-conservative
    2. Semi-discontinuous
    3. Bi-directional
    4. All of the above
(Ref. 1, pp. 406, 427)
  1. The function of SSB proteins in replication is to:
    1. Identify the origin of replication (ori)
    2. Relax the supercoils
    3. Unwind DNA
    4. Maintain DNA is unwound state after strand separation
(Ref. 1, p. 423)
  1. RNA primer:
    1. Is formed in eukaryotes but not in prokaryotes
    2. Primes replication of lagging strand but not the leading strand
    3. Contains ribothymidine instead of ribouridine
    4. None of the above
(Ref. 1, p. 424)
  1. RNA primer is replaced by deoxyribonucleotides after the:
    1. Addition of the first deoxyribonucleotide to the primer
    2. Formation of each Okazaki fragment
    3. Formation of several Okazaki fragments
    4. Complete replication of both the strands
(Ref. 1, pp. 425-426)
86 C
87 D
88 D
89 D
90 D
91 C
179
  1. Enhancer elements:
    1. Are the sites on DNA where RNA polymerase binds
    2. May be upstream or downstream from the gene regulated
    3. May be present on the same chromosome on which the regulated gene is present or on a different chromosome
    4. Are identified by the sigma factor
(Ref. 1, p. 477)
  1. During transcription, unwinding of DNA is catalysed by:
    1. Sigma factor
    2. RNA polymerase
    3. Helicase
    4. Rho factor
(Ref. 1, p. 438)
  1. In eukaryotes, the transcription factor that binds to TATA box is:
    1. TF II A
    2. TF II B
    3. TF II C
    4. TF II D
(Ref. 1, p.440)
  1. All the following statements about eukaryotic transcription are true except:
    1. TATA box is present upstream of every gene
    2. TATA box has a low melting temperature
    3. Transcription Factor II D (TF II D) binds to TATA box
    4. TF II D consists of TATA-binding protein (TBP) and TBP-associated factors (TAFs)
(Ref. 1, pp. 440-441)
  1. Intestinal apolipoprotein B is shorter than hepatic apolipoprotein B because:
    1. It is encoded by a different gene
    2. It is spliced in a different way
    3. RNA editing changes a sense codon into a nonsense codon
    4. It is cleaved after translation
(Ref. 1, p.449)
  1. The first event in post-transcriptional modification of RNA is:
    1. Addition of 7-methyl GTP cap
    2. Addition of poly-A tail
    3. Removal of introns and splicing
    4. Any of the above
(Ref. 1, p.436)
92 B
93 B
94 D
95 A
96 C
97 A
180
  1. Enhancer elements possess all the following properties except:
    1. They can work when located long distance from the promoter
    2. They may be upstream or downstream from the promoter
    3. They act on promoters located on the same DNA molecule
    4. They act on specific promoters
(Ref. 1, pp.477-478)
  1. Promoters and enhancers have the following similarity:
    1. They are specific for the genes they influence
    2. They influence genes located on the same DNA molecule
    3. They are located upstream from the genes they influence
    4. They may be located a long distance away from the genes they influence
(Ref. 1, p.477)
  1. The proteins that regulate gene expression must:
    1. Possess leucine zipper motif or zinc finger motif
    2. Possess a recognition domain and a domain that affects the transcription apparatus
    3. Bind to the promoter with high affinity
    4. Bind to the promoter with high specificity
(Ref. 1, pp. 480-483)
98 D
99 B
100 B

Genetic Code and Protein Synthesis15

  1. Anticodons are present on:
    1. Coding strand of DNA
    2. mRNA
    3. tRNA
    4. rRNA
(Ref. 1, p.410)
  1. Codons are present on:
    1. Non-coding strand of DNA
    2. hnRNA
    3. tRNA
    4. None of the above
(Ref. 1, pp. 403, 410)
  1. Nonsense codons are present on:
    1. mRNA
    2. tRNA
    3. rRNA
    4. None of the above
(Ref. 1, p. 455)
  1. Genetic code is said to be degenerate because:
    1. It can undergo mutations
    2. A large proportion of DNA is non-coding
    3. One codon can code for more than one amino acids
    4. More than one codons can code for the same amino acid
(Ref. 1, p. 453)
  1. All the following statements about genetic code are correct except:
    1. It is degenerate
    2. It is unambiguous
    3. It is nearly universal
    4. It is overlapping
(Ref. 1, p. 453)
1 C
2 B
3 A
4 D
5 D
182
  1. All the following statements about nonsense codons are true except:
    1. They do not code for amino acids
    2. They act as chain termination signals
    3. They are identical in nuclear and mitochondrial DNA
    4. They have no complementary anticodons
(Ref. 1, pp. 453, 463)
  1. A polycistronic mRNA can be seen in:
    1. Prokaryotes
    2. Eukaryotes
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 470)
  1. Non-coding sequences are present in the genes of:
    1. Bacteria
    2. Viruses
    3. Eukaryotes
    4. All of the above
(Ref. 1, pp. 416-417)
  1. Non-coding sequences in a gene are known as:
    1. Cistrons
    2. Nonsense codons
    3. Introns
    4. Exons
(Ref. 1, p. 416)
  1. Splice sites are present in:
    1. Prokaryotic mRNA
    2. Eukaryotic mRNA
    3. Eukalyotic hnRNA
    4. All of the above
(Ref. 1, p. 445)
  1. The common features of introns include all the following except:
    1. The base sequence begins with GU
    2. The base sequence ends with AG
    3. The terminal AG sequence is preceded by a purine-rich tract of ten nucleotides
    4. An adenosine residue in branch site participates in splicing
(Ref. 1, pp. 445-446)
  1. A spliceosome contains all the following except:
    1. hnRNA
    2. snRNAs
    3. Some proteins
    4. Ribosome
(Ref. 1, pp. 445-446)
6 C
7 A
8 C
9 C
10 C
11 C
12 D
183
  1. Self-splicing can occur in:
    1. Some precursors of rRNA
    2. Some precursors of tRNA
    3. hnRNA
    4. None of the above
(Ref. 2, pp. 864-865)
  1. Pribnow box is present in:
    1. Prokaryotic promoters
    2. Eukaryotic promoters
    3. Introns
    4. Exons
(Ref. 2, p. 101)
  1. Hogness box is present in:
    1. Prokaryotic promoters
    2. Eukaryotic promoters
    3. Introns
    4. Exons
(Ref. 2, p. 102)
  1. CAAT box is present in many:
    1. Prokaryotic promoters upstream of TATA box
    2. Prokaryotic promoters downstream of TATA box
    3. Eukaryotic promoters upstream of TATA box
    4. Eukaryotic promoters downstream of TATA box
(Ref. 1, pp. 440-441)
  1. Most of the eukaryotic promoters contain a:
    1. TATA box about 25 bp upstream of transcription start site
    2. CAAT box about 75 bp upstream of transcription start site
    3. Both of the above
    4. Neither of the above
(Ref. 2, p.102)
  1. All the following statements about tRNA are correct except:
    1. A given tRNA can be charged with only one particular amino acid
    2. The amino acid is recognised by the anticodon of tRNA
    3. The amino acid is attached to 3' end of tRNA
    4. The anticodon of tRNA finds the complementary codon on mRNA
(Ref. 1, pp. 454-455)
13 A
14 A
15 B
16 C
17 C
18 B
184
  1. All the following statements about charging of tRNA are correct except:
    1. It is catalysed by amino acyl tRNA synthetase
    2. ATP is converted into ADP and Pi in this reaction
    3. The enzyme recognises the tRNA and the amino acid
    4. There is a separate enzyme for each tRNA
(Ref. 1, pp. 454-455)
  1. All the following statements about recognition of a codon on mRNA by an anticodon on tRNA are correct except:
    1. The recognition of the third base of the codon is not very precise
    2. Imprecise recognition of the third base results in wobble
    3. More than one codons can be recognised by an anticodon due to Wobble
    4. Wobble results in incorporation of incorrect amino acids in the protein
(Ref. 1, p. 454)
  1. The first amino acyl tRNA which initiates translation in eukaryotes is:
    1. Methionyl tRNA
    2. Formylmethionyl tRNA
    3. Tyrosinyl tRNA
    4. Alanyl tRNA
(Ref. 1, p. 459)
  1. The first amino acyl tRNA which initiates translation in prokaryotes is:
    1. Methionyl tRNA
    2. Formylmethionyl tRNA
    3. Tyrosinyl tRNA
    4. Alanyl tRNA
(Ref. 2, p. 894)
  1. In eukaryotes, the 40 S pre-initiation complex contains all the following initiation factors except:
    1. eIF-1A
    2. eIF-2
    3. eIF-3
    4. eIF-4F
(Ref. 1, p. 460)
  1. Eukaryotic initiation factors 4A, 4B and 4F bind to:
    1. 40 S ribosomal subunit
    2. 60 S ribosomal subunit
    3. mRNA
    4. Amino acyl tRNA
(Ref. 1, p. 460)
19 B
20 D
21 A
22 B
23 D
24 C
185
  1. The codon which serves as translation start signal is:
    1. AUG
    2. UAG
    3. UGA
    4. UAA
(Ref. 1, pp. 459-461)
  1. The first amino acyl tRNA approaches 40 S ribosomal subunit in association with:
    1. eIF- 1A and GTP
    2. eIF-2 and GTP
    3. eIF-2C and GTP
    4. eIF-3 and GTP
(Ref. 1, p. 460)
  1. eIF-1A and eIF-3 are required:
    1. For binding of amino acyl tRNA to 40 S ribosomal subunit
    2. For binding of mRNA to 40 S ribosomal subunit
    3. For binding of 60 S subunit to 40 S subunit
    4. To prevent binding of 60S subunit to 40 S subunit
(Ref. 1, p. 459)
  1. eIF-4A possesses:
    1. ATPase activity
    2. GTPase activity
    3. Helicase activity
    4. None of the above
(Ref. 1, p. 459)
  1. eIF-4B:
    1. Binds to chain initiation codon on mRNA
    2. B. Binds to 3' end of mRNA
    3. Binds to 5' end of mRNA
    4. D. Unwinds mRNA near its 5' end
(Ref. 1, p. 459)
  1. Peptidyl transferase activity is present in:
    1. 40 S ribosomal subunit
    2. 60 S ribosomal subunit
    3. eEF-2
    4. Amino acyl tRNA
(Ref. 1, p. 463)
  1. After formation of a peptide bond, mRNA is translocated along the ribosome by:
    1. eEF-1 and GTP
    2. eEF-2 and GTP
    3. Peptidyl transferase and GTP
    4. Peptidyl transferase and ATP
(Ref. 1, p. 463)
25 A
26 B
27 D
28 A
29 D
30 B
31 B
186
  1. Binding of formylmethionyl tRNA to 30 S ribosomal subunit of prokaryotes is inhibited by:
    1. Streptomycin
    2. Chloramphenicol
    3. Erythromycin
    4. Mitomycin
(Ref. 2, p. 903)
  1. Tetracyclines inhibit binding of amino acyl tRNAs to:
    1. 30 S ribosomal subunits
    2. 40 S ribosomal subunits
    3. 50 S ribosomal subunits
    4. 60 S ribosomal subunits
(Ref. 2, p. 903)
  1. Peptidyl transferase activity 50 S of ribosomal subunits is inhibited by:
    1. Rifampicin
    2. Cycloheximide
    3. Chloramphenicol
    4. Erythromycin
(Ref. 2, p. 903)
  1. Erythromycin binds to 50 S ribosomal subunit and:
    1. Inhibits binding of amino acyl tRNA
    2. Inhibits peptidyl transferase activity
    3. Inhibits translocation
    4. Causes premature chain termination
(Ref. 2, p. 903)
  1. Puromycin causes premature chain termination in:
    1. Prokaryotes
    2. Eukaryotes
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 446)
  1. Diphtheria toxin inhibits:
    1. Prokaryotic EF-1
    2. Prokaryotic EF-2
    3. Eukaryotic EF-1
    4. Eukaryotic EF-2
(Ref. 1, p. 466)
  1. The proteins destined to be transported out of the cell have all the following features except:
    1. They possess a signal sequence
    2. Ribosomes synthesising them are bound to endoplasmic reticulum
    3. After synthesis, they are delivered into Golgi apparatus
    4. They are tagged with ubiquitin
(Ref. 1, pp. 517-519)
32 A
33 A
34 C
35 C
36 C
37 D
38 D
187
  1. SRP receptors involved in protein export are present on:
    1. Ribosomes
    2. Endoplasmic reticulum
    3. Golgi apparatus
    4. Cell membrane
(Ref. 1, p. 519)
  1. The signal sequence of proteins is cleaved off:
    1. On the ribosomes immediately after synthesis
    2. In the endoplasmic reticulum
    3. During processing in Golgi apparatus
    4. During passage through the cell membrane
(Ref. 1, p. 519)
  1. The half-life of a protein depends upon its:
    1. Signal sequence
    2. N-terminus amino acid
    3. C-terminus amino acid
    4. Prosthetic group
(Ref. 2, p. 912)
  1. Besides structural genes that encode proteins, DNA contains some regulatory sequences which are known as:
    1. Operons
    2. Cistrons
    3. cis-Acting elements
    4. trans-Acting factors
(Ref. 1, p. 477)
  1. Inducers and repressors are:
    1. Enhancer and silencer elements respectively
    2. trans-Acting factors
    3. cis-Acting elements
    4. Regulatory proteins
(Ref. 1, pp. 471, 477)
  1. cis-Acting elements include:
    1. Steroid hormones
    2. Calcitriol
    3. Histones
    4. Enhancers
(Ref. 1, p. 477)
  1. Enhancer elements:
    1. Are trans-Acting factors
    2. Are present between promoters and the structural genes
    3. Increase the expression of some structural genes
    4. Encode specific enhancer proteins
(Ref. 1, p. 477)
39 B
40 B
41 B
42 C
43 B
44 D
45 C
188
  1. trans-Acting factors include:
    1. Promoters
    2. Repressors
    3. Enhancers
    4. Silencers
(Ref. 1, p. 477)
  1. Enhancer elements have all the following features except:
    1. They increase gene expression through a promoter
    2. Each enhancer activates a specific promoter
    3. They may be located far away from the promoter
    4. They may be upstream or downstream from the promoter
(Ref. 1, p. 477)
  1. Amplification of dihydrofolate reductase gene may be brought about by:
    1. High concentrations of folic acid
    2. Deficiency of folic acid
    3. Low concentrations of thymidylate
    4. Methotrexate
(Ref. 1, p. 484)
  1. Proteins which interact with DNA and affect the rate of transcription possess the following structural motif:
    1. Helix-turn-helix motif
    2. Zinc finger motif
    3. Leucine zipper motif
    4. Any of the above
(Ref. 1, p. 480)
  1. Lac operon is a cluster of genes present in:
    1. Human beings
    2. E.coli
    3. Lambda phage
    4. All of the above
(Ref. 1, p. 470)
  1. Lac operon is a cluster of:
    1. Three structural genes
    2. Three structural genes and their promoter
    3. A regulatory gene, an operator and a promoter
    4. A regulatory gene, an operator, a promoter and three structural genes
(Ref. 1, p. 470)
46 B
47 B
48 D
49 D
50 B
51 D
189
  1. The regulatory i gene of lac operon:
    1. Is inhibited by lactose
    2. Is inhibited by its own product, the repressor protein
    3. Forms a regulatory protein which increases the expression of downstream structural genes
    4. Is constitutively expressed
(Ref. 1, p. 471)
  1. RNA polymerase holoenzyme binds to lac operon at the following site:
    1. i gene
    2. z gene
    3. Operator locus
    4. Promoter region
(Ref. 1, p. 471)
  1. Transcription of z, y and a genes of lac operon is prevented by:
    1. Lactose
    2. Allo-lactose
    3. Repressor
    4. cAMP
(Ref. 1, p. 471)
  1. Transcription of structural genes of lac operon is prevented by binding of the repressor tetramer to:
    1. i gene
    2. Operator locus
    3. Promoter
    4. z gene
(Ref. 1, p. 471)
  1. The enzymes encoded by z, y and a genes of lac operon are inducible, and their inducer is:
    1. Lactose
    2. B. Allo-lactose
    3. Catabolite gene activator protein
    4. All of the above
(Ref. 2, p. 960)
  1. Binding of RNA polymerase holoenzyme to the promoter region of lac operon is facilitated by:
    1. Catabolite gene activator protein (CAP)
    2. cAMP
    3. CAP-cAMP complex
    4. None of the above
(Ref. 1, p. 471)
52 D
53 D
54 C
55 B
56 B
57 C
190
  1. Lactose or its analogues act as positive regulators of lac operon by:
    1. Attaching to i gene and preventing its expression
    2. Increasing the synthesis of catabolite gene activator protein
    3. Attaching to promoter region and facilitating the binding of RNA polymerase holoenzyme
    4. Binding to repressor subunits so that the repressor cannot attach to the operator locus
(Ref. 1, p. 471)
  1. Expression of structural genes of lac operon is affected by all of the following except:
    1. Lactose or its analogues
    2. Repressor tetramer
    3. cAMP
    4. CAP-cAMP complex
(Ref. 1, pp. 470-472)
  1. The coding sequences in lac operon include:
    1. i gene
    2. i gene, operator locus and promoter
    3. z, y and a genes
    4. i, z, y and a genes
(Ref. 1, pp. 470-471)
  1. Mutations can be caused by:
    1. Ultraviolet radiation
    2. Ionising radiation
    3. Alkylating agents
    4. All of the above
(Ref. 3, pp. 914-916)
  1. Mutations can be caused by:
    1. Nitrosamine
    2. Dimethyl sulphate
    3. Acridine
    4. All of the above
(Ref. 3, pp. 916, 921)
  1. Nitrous oxide can deaminate:
    1. Cytosine to form uracil
    2. Adenine to form hypoxanthine
    3. Guanine to form xanthine
    4. All of the above
(Ref. 2, p. 811)
  1. Exposure of DNA to ultraviolet radiation can lead to the formation of:
    1. Adenine dimers
    2. Guanine dimers
    3. Thymine dimers
    4. Uracil dimers
(Ref. 1, p. 430)
58 D
59 C
60 D
61 D
62 D
63 A
64 C
191
  1. Damage to DNA caused by ultraviolet radiation in E.coli is repaired by:
    1. uvr ABC excinuclease
    2. DNA polymerase I
    3. DNA ligase
    4. All the three acting sequentially
(Ref. 2, p. 811)
  1. Xeroderma pigmentosum results from a defect in:
    1. Excinuclease that removes pyrimidine dimers
    2. DNA polymerase β
    3. DNA ligase
    4. Any of the above
(Ref. 2, p.813)
  1. All the following statements about xeroderma pigmentosum are true except:
    1. It is a genetic disease
    2. Its inheritence is autosomal dominant
    3. Excinuclease that removes pyrimidine dimers is defective in this disease
    4. It results in multiple skin cancers
(Ref. 2, p. 813)
  1. Substitution of an adenine base by guanine in DNA is known as:
    1. Transposition
    2. Transition
    3. Transversion
    4. Frameshift mutation
(Ref. 1, p. 455)
  1. Substitution of a thymine base by adenine in DNA is known as:
    1. Transposition
    2. Transition
    3. Transversion
    4. Frameshift mutation
(Ref. 1, p. 455)
  1. A point mutation results from:
    1. Substitution of a base
    2. Insertion of a base
    3. Deletion of a base
    4. Any of the above
(Ref. 1, p. 455)
  1. Substitution of a base can result in a:
    1. Silent mutation
    2. Mis-sense mutation
    3. Nonsense mutation
    4. Any of the above
(Ref. 1, pp. 455-456)
65 D
66 A
67 B
68 B
69 C
70 A
71 D
192
  1. A silent mutation is most likely to result from:
    1. Substitution of the first base of a codon
    2. Substitution of the third base of a codon
    3. Conversion of a nonsense codon into a sense codon
    4. Conversion of a sense codon into a nonsense codon
(Ref. 1, pp. 455-456)
  1. The effect of a mis-sense mutation can be:
    1. Acceptable
    2. Partially acceptable
    3. Unacceptable
    4. Any of the above
(Ref. 1, p. 455)
  1. Amino acid sequence of the encoded protein is not changed in:
    1. Silent mutation
    2. Acceptable mis-sense mutation
    3. Both of the above
    4. Neither of the above
(Ref. 1, pp. 455-456)
  1. Haemoglobin S is an example of a/an:
    1. Silent mutation
    2. Acceptable mis-sense mutation
    3. Unacceptable mis-sense mutation
    4. Partially acceptable mis-sense mutation
(Ref. 1, pp. 456-457)
  1. If the codon UAC on mRNA changes into UAG as a result of a base substitution in DNA, it will result in:
    1. Silent mutation
    2. Acceptable mis-sense mutation
    3. Nonsense mutation
    4. Frameshift mutation
(Ref. 1, pp. 453, 456)
  1. Insertion of a base in a gene can cause:
    1. Change in reading frame
    2. Garbled amino acid sequence in the encoded protein
    3. Premature termination of translation
    4. All of the above
(Ref. 1, pp. 457-458)
72 B
73 D
74 A
75 D
76 C
77 D
193
  1. A frameshift mutation changes the reading frame because the genetic code:
    1. Is degenerate
    2. Is overlapping
    3. Has no punctuations
    4. Is universal
(Ref. 1, p. 457)
  1. Suppressor mutations occur in:
    1. Structural genes
    2. Promoter regions
    3. Silencer elements
    4. Anticodons of tRNA
(Ref. 1, pp. 458-459)
  1. Suppressor tRNAs can neutralise the effects of mutations in:
    1. Structural genes
    2. Promoter regions
    3. Enhancer elements
    4. All of the above
(Ref. 1, p. 458)
  1. Mutations in promoter regions of genes can cause:
    1. Premature termination of translation
    2. Change in reading frame of downstream structural gene
    3. Decreased efficiency of transcription
    4. All of the above
(Ref. 1, p. 440)
  1. Mitochondrial protein synthesis is inhibited by:
    1. Cycloheximide
    2. B. Chloramphenicol
    3. C. Diphtheria toxin
    4. None of the above
(Ref. 3, pp. 894-895)
  1. All the following statements about puromycin are true except:
    1. It is an alanyl tRNA analogue
    2. It causes premature termination of protein synthesis
    3. It inhibits protein synthesis in prokaryotes
    4. It inhibits protein synthesis in eukaryotes
(Ref. 1, p. 466)
78 C
79 D
80 A
81 C
82 B
83 A
194
  1. Leucine zipper motif is seen in some helical proteins when leucine residues appear at every:
    1. Third position
    2. Fifth position
    3. Seventh position
    4. Ninth position
(Ref. 1, p. 482)
  1. Zinc finger motif is formed in some proteins by binding of zinc to:
    1. Two cysteine residues
    2. Two histidine residues
    3. Two arginine residues
    4. Two cysteine and two histidine residues or two pairs of two cysteine residues each
(Ref. 1, p. 481)
  1. Genetic code is identical in all the following except:
    1. Nuclear DNA
    2. Mitochondrial DNA
    3. Bacterial DNA
    4. Viral DNA
(Ref. 1, p.453)
  1. Genetic code is said to be unambiguous because:
    1. It is universal in all living organisms
    2. The same four bases form codons in all living organisms
    3. A codon codes for only one amino acid
    4. Each amino acid is encoded by a single codon
(Ref. 1, p.453)
  1. Mitochondrial DNA is inherited from:
    1. Father
    2. Mother
    3. Either of the above
    4. Both of the above
(Ref. 1, p.836)
  1. Deletion of a single base from a structural gene can cause the following abnormality in the encoded protein:
    1. Garbled amino acid sequence
    2. An abnormally small protein
    3. An abnormally large protein
    4. Any of the above
(Ref. 1, p. 457)
84 C
85 D
86 B
87 C
88 B
89 D
195
  1. After formation of the initiation complex in eukaryotes:
    1. Methionyl tRNA occupies the A site on the ribosome
    2. 7-Methylguanosine triphosphate cap is split off
    3. Poly-A tail is split off
    4. None of the above
(Ref. 1, p.460)
  1. All of the following are required for initiation of translation in eukaryotes except:
    1. mRNA
    2. Formylmethionyl tRNA
    3. GTP
    4. Ribosome
(Ref. 1, p.460)
  1. All of the following are required for initiation of translation in prokaryotes except:
    1. hnRNA
    2. Formylmethionyl tRNA
    3. GTP
    4. Ribosome
(Ref. 2, p.896)
  1. The following can inhibit initiation of translation in prokaryotes:
    1. Streptomycin
    2. Chloramphenicol
    3. Erythromycin
    4. Puromycin
(Ref. 2, p.903)
  1. Signal peptidase is present in:
    1. Nucleus
    2. Mitochondria
    3. Endoplasmic reticulum
    4. Lysosomes
(Ref. 1, p.519)
  1. The number of high-energy phosphate bonds spent for the formation of each peptide bond of proteins is:
    1. One
    2. Two
    3. Three
    4. Four
(Ref. 1, p.463)
  1. All the following statements about elongation are true except:
    1. The new incoming amino acyl tRNA occupies the A site on the ribosome
    2. A peptide bond is formed between the carboxyl group of the new amino acid and the amino group of the last amino acid
    3. No energy is spent in forming the peptide bond
    4. Formation of peptide bond is catalysed by a ribozyme
(Ref. 1, pp. 461-462)
90 D
91 B
92 A
93 A
94 C
95 D
96 B
196
  1. All the following statements about eukaryotic translation are true except:
    1. Translation begins with methionine
    2. There is only one codon for methionine
    3. There is only one tRNA for methionine for initiating translation and for adding internal methionine residues in the protein
    4. In mitochondrial DNA, the codon for methionine is different from that in nuclear DNA
(Ref. 1, pp. 453, 459)
  1. All the following statements about eukaryotic peptidyl transferase are true except:
    1. It is present in the 60S ribosomal subunit
    2. It is a ribozyme
    3. It hydrolyses GTP into GDP and Pi for forming the peptide bond
    4. It is inhibited by cycloheximide
(Ref. 1, pp. 463, 466)
  1. Diphtheria toxin inhibits:
    1. Initiation of protein synthesis
    2. Elongation of protein being synthesised
    3. Insertion of protein into endoplasmic reticulum
    4. Transport of protein out of the cell
(Ref. 1, p.466)
  1. The following component targets the proteins to lysosomes:
    1. Signal peptide
    2. KDEL sequence
    3. Mannose-6-phosphate
    4. Sialic acid
(Ref. 1, p. 521)
97 C
98 C
99 B
100 C

Recombinant DNA Technology16

  1. Restriction endonucleases are present in:
    1. Viruses
    2. Bacteria
    3. Eukaryotes
    4. All of the above
(Ref. 1, p. 489)
  1. Restriction endonucleases split:
    1. RNA
    2. Single-stranded DNA
    3. Double-stranded DNA
    4. DNA-RNA hybrids
(Ref. 1, p. 490)
  1. Restriction endonucleases can recognise:
    1. Palindromic sequences
    2. Chimeric DNA
    3. DNA-RNA hybrids
    4. Homopolymer sequences
(Ref. 1, p. 491)
  1. All of the following statements about restriction endonucleases are true except:
    1. They are present in bacteria
    2. They act on double-stranded DNA
    3. They recognise palindromic sequences
    4. They always produce sticky ends
(Ref. 1, pp. 489-491)
1 B
2 C
3 A
4 D
198
  1. The following is a palindromic sequence:
    1. 5'—GGGGGG—3'
      3'—CCCCCC—5'
    2. 5'—ATGCAG—3'
      3'—TACGTC—5'
    3. 5'—GGCGCC—3'
      3'—CCGCGG—5'
    4. 5'—CGAAGC—3'
      3'—GCTTCG—5'
(Ref. 1, p. 491)
  1. In sticky ends produced by restriction endonucleases:
    1. The two strands of DNA are joined to each other
    2. The DNA strands stick to the restriction endonuclease
    3. The ends of a double-stranded fragment are overlapping
    4. The ends of a double-stranded fragment are non-over-lapping
(Ref 1, p. 490)
  1. All of the following may be used as expression vectors except:
    1. Plasmid
    2. Bacteriophage
    3. Baculovirus
    4. E. coli
(Ref. 2, pp. 136-137)
  1. A plasmid is a:
    1. Single-stranded linear DNA
    2. Single-stranded circular DNA
    3. Double-stranded linear DNA
    4. Double-stranded circular DNA
(Ref. 1, p. 491)
  1. Fragments of DNA can be identified by the technique of:
    1. Western blotting
    2. Eastern blotting
    3. Northern blotting
    4. Southern blotting
(Ref. 1, p. 494)
  1. A particular RNA in a mixture can be identified by:
    1. Western blotting
    2. Eastern blotting
    3. Northern blotting
    4. Southern blotting
(Ref. 1, p. 494)
5 C
6 C
7 D
8 D
9 D
10 C
199
  1. A radioactive isotope labelled cDNA probe is used in:
    1. Southern blotting
    2. Northern blotting
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 495)
  1. An antibody probe is used in:
    1. Southern blotting
    2. Northern blotting
    3. Western blotting
    4. None of the above
(Ref. 1, p. 495)
  1. A particular protein in a mixture can be detected by:
    1. Southern blotting
    2. Northern blotting
    3. Western blotting
    4. None of the above
(Ref. 2, p. 122)
  1. The first protein synthesised by recombinant DNA technology was:
    1. Streptokinase
    2. Human growth hormone
    3. Tissue plasminogen activator
    4. Human insulin
(Ref. 1, p. 611)
  1. For production of a eukaryotic protein by recombinant DNA technology in bacteria, the template used is:
    1. Eukaryotic gene
    2. hnRNA
    3. mRNA
    4. Any of the above
(Ref. 2, p. 135)
  1. Trials for gene therapy in human beings were first carried out, with considerable success, in a genetic disease called:
    1. Cystic fibrosis
    2. Thalassaemia
    3. Adenosine deaminase deficiency
    4. Lesch-Nyhan syndrome
(Ref. 2, p. 141)
  1. Chimeric DNA:
    1. Is found in bacteriophages
    2. Contains unrelated genes
    3. Has no restriction sites
    4. Is palindromic
(Ref. 2, p. 127)
11 C
12 C
13 C
14 D
15 C
16 C
17 B
200
  1. The following may be used as a cloning vector:
    1. Prokaryotic plasmid
    2. Lambda phage
    3. Cosmid
    4. All of the above
(Ref. 1, pp. 491-492)
  1. The plasmid pBR 322 has:
    1. Ampicillin resistance gene
    2. Tetracycline resistance gene
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 494)
  1. Lambda phage can be used to clone DNA fragments of the size:
    1. Upto 3 kilobases
    2. Upto 20 kilobases
    3. Upto 45 kilobases
    4. Upto 1,000 kilobases
(Ref. 1, p. 492)
  1. Cosmids can be used to clone DNA fragments of the size:
    1. 1,000 kb
    2. 100 kb
    3. 45 kb
    4. None of the above
(Ref. 2, p. 129)
  1. A cosmid is a:
    1. Large bacterial plasmid
    2. Viral plasmid
    3. Hybrid of plasmid and phage
    4. Yeast plasmid
(Ref. 2, p. 132)
  1. Polymerase chain reaction can rapidly amplify DNA sequences of the size:
    1. Upto 10 kilobases
    2. Upto 45 kilobases
    3. Upto 100 kilobases
    4. Upto 1,000 kilobases
(Ref. 1, p. 496)
  1. The DNA polymerase commonly used in polymerase chain reaction is obtained from:
    1. E. coli
    2. Yeast
    3. T. aquaticus
    4. Eukaryotes
(Ref. 1, p. 496)
18 D
19 C
20 B
21 C
22 C
23 A
24 C
201
  1. Base sequence of DNA can be determined by:
    1. Maxam-Gilbert method
    2. Sanger's dideoxy method
    3. Either of the above
    4. Neither of the above
(Ref. 1, p. 495)
  1. From a DNA-RNA hybrid, DNA can be obtained by addition of:
    1. dna B protein and ATP
    2. Helicase and ATP
    3. DNA topoisomerase I
    4. Alkali
(Ref. 2, p. 136)
  1. Optimum temperature of DNA polymerase of T. aquaticus is:
    1. 30 C
    2. 37 C
    3. 54 C
    4. 72 C
(Ref. 2, p. 133)
  1. In addition to Taq polymerase, polymerase chain reaction requires all of the following except:
    1. template DNA
    2. Deoxyribonucleoside triphosphates
    3. Primers
    4. Primase
(Ref. 2, p. 133)
  1. DNA polymerase of T. aquaticus is preferred to that of E. coli in PCR because:
    1. It replicates DNA more efficiently
    2. It doesn't require primers
    3. It is not denatured at the temperature at which the DNA strands separate
    4. It doesn't cause errors in replication
(Ref. 1, p. 495)
  1. Twenty cycles of PCR can amplify DNA:
    1. 220 fold
    2. 202 fold
    3. 20 2 fold
    4. 20 fold
(Ref. 2, p. 134)
  1. Transgenic animals may be prepared by introducing a foreign gene into:
    1. Somatic cells of young animals
    2. Testes and ovaries of animals
    3. A viral vector and infecting the animals with the viral vector
    4. Fertilised egg and implanting the egg into a foster mother
(Ref. 1, p. 502)
25 C
26 D
27 D
28 D
29 C
30 A
31 D
202
  1. DNA fragments of 1,000 kb can be cloned with the vector:
    1. Bacterial plasmid
    2. Lambda phage
    3. Cosmid
    4. Yeast artificial chromosome
(Ref. 2, p.132)
  1. DNA finger printing is based on the presence in DNA of:
    1. Constant number of tandem repeats
    2. Variable number of tandem repeats
    3. Non-repetitive sequences in each DNA
    4. Introns in eukaryotic DNA
(Ref. 1, p. 501)
  1. All the following statements about restriction fragment length polymorphism are true except:
    1. It results from mutations in restriction sites
    2. Mutations in restriction sites can occur in coding or non-coding regions of DNA
    3. It is inherited in Mendelian fashion
    4. It can be used to diagnose any genetic disease
(Ref. 1, p. 500)
  1. Terminal transferase:
    1. Removes nucleotides from 3' end
    2. Adds nucleotides at 3' end
    3. Removes nucleotides from 5' end
    4. Adds nucleotides at 5' end
(Ref. 1, p. 492)
  1. S 1 nuclease hydrolyses:
    1. DNA of somatic cells
    2. DNA of sperms
    3. Any double stranded DNA
    4. Any single stranded DNA
(Ref. 1, p. 492)
  1. A particular segment of DNA can be clipped out by using:
    1. Polymerase chain reaction
    2. Deoxyribonuclease
    3. Restriction endonucleases
    4. Cosmids
(Ref. 1, p. 502)
32 D
33 B
34 D
35 B
36 D
37 C
203
  1. An mRNA transcript is used as template for expression of a eukaryotic gene in a prokaryote because:
    1. It is difficult to introduce a eukaryotic gene in prokaryotic DNA
    2. mRNA does not have introns
    3. Prokaryotic deoxyribonuclease would hydrolyse the eukaryotic gene
    4. Prokaryotes have RNA genomes
(Ref. 2, p.135)
  1. Recombinant DNA can not be prepared without:
    1. Plasmids
    2. Restriction enzymes producing sticky ends
    3. DNA polymerase III holoenzyme
    4. DNA ligase
(Ref. 1, pp.490-491)
  1. When a DNA molecule is treated with a particular restriction endonuclease, it is split into:
    1. Two fragments having identical base sequences at the split ends
    2. Two fragments having different base sequences at the split ends
    3. Many fragments having identical base sequences at the split ends
    4. Many fragments having different base sequences at the split ends
(Ref. 1, p. 490)
  1. The function of plasmids in a bacterium is to:
    1. Enable the bacterium to infect other cells easily
    2. Destroy viruses that have entered the bacterial cell
    3. Provide antibiotic resistance to the bacterium
    4. Help the bacterium to multiply rapidly
(Ref. 1, pp. 491-492)
  1. All the following statements about bacterial plasmids are true except:
    1. They replicate together with bacterial DNA
    2. They possess restriction sites
    3. They possess antibiotic -resistance genes
    4. They can accept foreign DNA
(Ref. 1, pp. 491-492)
38 B
39 D
40 C
41 C
42 A
204
  1. Plasmids and phages have the following difference:
    1. DNA of plasmids is linear while that of phages is circular
    2. Plasmid DNA is double-stranded while that of phages is single-stranded
    3. Plasmids possess antibiotic-resistance genes while phages do not
    4. Plasmids can accept foreign DNA of larger size than phages
(Ref. 1,pp.491-492)
  1. All the following statements about cosmids are true except:
    1. Their DNA is double-stranded and circular
    2. Their DNA is integrated into host cell DNA for replication
    3. They possess cos sites
    4. They can accept foreign DNA of larger size than plasmids
(Ref. 1, p.492)
  1. For inserting foreign DNA in the increasing order of size, the correct sequence of vectors is:
    1. Plasmids, phages and cosmids
    2. Phages, plasmids and cosmids
    3. Cosmids, plasmids and phages
    4. Plasmids, cosmids and phages
(Ref. 1, p.493)
  1. For preparing a genomic library of an organism, one requires:
    1. Isolation of all the mRNAs from a tissue
    2. Preparation of cDNA copies of all mRNAs by reverse transcription
    3. Preparation of double-stranded DNAs from cDNAs
    4. None of the above
(Ref. 1, p.493)
  1. Northern blotting requires all the following except:
    1. RNA
    2. Gel electrophoresis
    3. Labelled cDNA probe
    4. Restriction enzymes
(Ref. 1, p.495)
43 C
44 B
45 A
46 D
47 D
205
  1. In Maxam-Gilbert method of DNA sequencing:
    1. DNA to be sequenced is used as template for synthesising cDNA
    2. cDNA synthesis is interrupted by dideoxyribonuc-leotides
    3. DNA molecule to be sequenced is cleaved at specific sites enzymatically
    4. DNA molecule to be sequenced is cleaved at specific sites chemically
(Ref. 1, p.495)
  1. In Sanger's method of DNA sequencing:
    1. DNA to be sequenced is used as a template for synthesising cDNA
    2. cDNA synthesis is interrupted by using dideoxyribonucleotides
    3. Labelled deoxynucleoside triphosphates are used as substrates
    4. All of the above
(Ref. 2, p.123)
  1. A cDNA probe can be labeled with 32P at the 5'-end by:
    1. Terminal transferase
    2. S 1 nuclease
    3. Polynucleotide kinase
    4. DNA ligase
(Ref. 1, p.492)
  1. A particular gene on a large piece of DNA can be located by:
    1. Chromosome walking
    2. DNA finger printing
    3. Plaque hybridisation
    4. Targeted gene knockout
(Ref. 1, p.500)
48 D
49 D
50 C
51 A

Metabolism of Amino Acids17

  1. Positive nitrogen balance is seen in:
    1. Starvation
    2. Wasting diseases
    3. Growing age
    4. Intestinal malabsorption
(Ref. 1, pp. 313, 655)
  1. Alanine can be synthesised from:
    1. Glutamate and α-ketoglutarate
    2. Pyruvate and glutamate
    3. Pyruvate and α-ketoglutarate
    4. Aspartate and α-ketoglutarate
(Ref. 1, p.308)
  1. All of the following are required for synthesis of alanine except:
    1. Pyruvate
    2. α-Ketoglutarate
    3. Glutamate
    4. Pyridoxal phosphate
(Ref. 1, pp. 308, 315)
  1. All the following statements about aspartate are true except:
    1. It is a non-essential amino acid
    2. It is a dicarboxylic amino acid
    3. It can be synthesised from pyruvate and glutamate
    4. It can be converted into asparagine
(Ref. 1, p. 308)
  1. Glycine can be synthesised from:
    1. Serine
    2. Choline
    3. Betaine
    4. All of the above
(Ref. 1, pp. 309, 310)
1 C
2 B
3 B
4 C
5 D
207
  1. All of the following are required for synthesis of glutamine except:
    1. Glutamate
    2. Ammonia
    3. Pyridoxal phosphate
    4. ATP
(Ref. 1, p. 308)
  1. A coenzyme required for the synthesis of glycine from serine is:
    1. ATP
    2. Pyridoxal phosphate
    3. Tetrahydrofolate
    4. NAD
(Ref. 1, p. 310)
  1. All the following statements about proline are true except:
    1. It is an imino acid
    2. It can be synthesised from glutamate
    3. It can be catabolised to glutamate
    4. Free proline can be hydroxylated to hydroxyproline
(Ref. 1, pp. 310-311)
  1. A protein rich in hydroxyproline is:
    1. Prolamin
    2. Procollagen
    3. Collagen
    4. Proinsulin
(Ref. 1, p. 311)
  1. All the following statement about hydroxyproline are true except:
    1. There is no codon for hydroxyproline
    2. It is present in large amounts in collagen
    3. Free proline cannot be hydroxylated to hydroxyproline
    4. Hydroxylation of proline residues is catalysed by a dioxygenase
(Ref. 1, p. 311)
  1. All of the following are required for hydroxylation of proline residues except:
    1. Ascorbic acid
    2. Glutamate
    3. Ferrous ions
    4. Molecular oxygen
(Ref. 1, p. 311)
  1. Cysteine can be synthesised from methionine and:
    1. Serine
    2. Homoserine
    3. Homocysteine
    4. Threonine
(Ref. 1, p. 310)
6 C
7 C
8 D
9 C
10 D
11 B
12 A
208
  1. Methionine is synthesised in human body from:
    1. Cysteine and homoserine
    2. Homocysteine and serine
    3. Cysteine and serine
    4. None of the above
(Ref. 1, p. 307)
  1. Hydroxylation of phenylalanine requires all of the following except:
    1. Phenylalanine hydroxylase
    2. Tetrahydrobiopterin
    3. NADH
    4. Molecular oxygen
(Ref. 1, p. 311)
  1. During catabolism of amino acids, their amino groups are transferred mainly to:
    1. Pyruvate
    2. Oxaloacetate
    3. α-Ketoglutarate
    4. Ornithine
(Ref. 1, p. 316)
  1. The amino acid that undergoes oxidative deamination at a significant rate is:
    1. Alanine
    2. Aspartate
    3. Glutamate
    4. Glutamine
(Ref. 1, p. 316)
  1. Allosteric inhibitor of glutamate dehydrogenase is:
    1. ATP
    2. ADP
    3. AMP
    4. GMP
(Ref. 1, p.316)
  1. Allosteric activator of glutamate dehydrogenase is:
    1. ATP
    2. GTP
    3. ADP and GDP
    4. AMP and GMP
(Ref. 2, p. 630)
  1. Free ammonia is released during:
    1. Oxidative deamination of glutamate
    2. Catabolism of purines
    3. Catabolism of pyrimidines
    4. All of the above
(Ref. 1, pp. 316, 396, 399)
13 D
14 C
15 C
16 C
17 A
18 C
19 D
209
  1. An organ which is extremely sensitive to ammonia toxicity is:
    1. Liver
    2. Brain
    3. Kidney
    4. Heart
(Ref. 1, p. 317)
  1. Ammonia is transported from muscles to liver mainly in the form of:
    1. Free ammonia
    2. Glutamine
    3. Asparagine
    4. Alanine
(Ref. 1, p. 318)
  1. Immediate detoxification of ammonia is done in brain by fixing it in the form of:
    1. Glutamine
    2. Alanine
    3. Aspartate
    4. Asparagine
(Ref. 1, p. 317)
  1. All the following statements about glutamine are true except:
    1. Glutamine is formed solely to detoxify ammonia
    2. Synthesis of glutamine from glutamate and ammonia requires energy
    3. Renal tubular cells are a major site for breakdown of glutamine
    4. Glutamine can be incorporated in proteins
(Ref. 1, pp. 317-318, 453)
  1. The major site of urea synthesis is:
    1. Brain
    2. Kidneys
    3. Liver
    4. Muscles
(Ref. 1, p. 319)
  1. The carbon atom of urea is provided by:
    1. Carbon dioxide
    2. Aspartate
    3. Ornithine
    4. None of the above
(Ref. 1, p. 320)
  1. The nitrogen atoms of urea are provided by:
    1. Ammonia
    2. Ammonia and alanine
    3. Ammonia and aspartate
    4. Ammonia and ornithine
(Ref. 1, p. 320)
20 B
21 D
22 A
23 A
24 C
25 A
26 C
210
  1. The number of high-energy phosphate bonds utilised for synthesis of one molecule of urea is:
    1. One
    2. Two
    3. Three
    4. Four
(Ref. 1, p. 320)
  1. Carbamoyl phosphate required for urea synthesis is formed in:
    1. Cytosol
    2. Mitochondria
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 320)
  1. Cytosolic and mitochondrial carbamoyl phosphate synthetase have the following similarity:
    1. Both use ammonia as a substrate
    2. Both provide carbamoyl phosphate for urea synthesis
    3. Both require N-acetylglutamate as an activator
    4. Both are allosteric enzymes
(Ref. 1, pp. 319, 393-394)
  1. Energy spent for the synthesis of carbamoyl phosphate is:
    1. Nil
    2. One high-energy phosphate bond
    3. Two high-energy phosphate bonds
    4. Three high-energy phosphate bonds
(Ref. 1, p. 320)
  1. For the synthesis of citrulline:
    1. Carbamoyl phosphate moves from mitochondria to cytosol
    2. Carbamoyl phosphate moves from cytosol to mitochondria
    3. Ornithine moves from mitochondria to cytosol
    4. Ornithine moves from cytosol to mitochondria
(Ref. 1, p. 319)
  1. The following enzyme of urea cycle is present in cytosol:
    1. Argininosuccinic acid synthetase
    2. Argininosuccinase
    3. Arginase
    4. All of the above
(Ref. 1, p. 320)
27 D
28 B
29 D
30 C
31 D
32 D
211
  1. During the synthesis of argininosuccinic acid:
    1. One ATP is converted into ADP and Pi
    2. One ATP is converted into AMP and PPi
    3. One GTP is converted into GDP and Pi
    4. No energy is required
(Ref. 1, p. 320)
  1. During the conversion of citrulline into arginine via argininosuccinate, aspartate is converted into:
    1. Oxaloacetate
    2. Fumarate
    3. Malate
    4. Asparagine
(Ref. 1, p. 320)
  1. ATP is required in following reactions of urea cycle:
    1. Synthesis of carbamoyl phosphate and citrulline
    2. Synthesis of citrulline and argininosuccinate
    3. Synthesis of argininosuccinate and arginine
    4. Synthesis of carbamoyl phosphate and argininosuccinate
(Ref. 1, p. 320)
  1. Daily excretion of nitrogen by an adult man is about:
    1. 15-20 mg
    2. 1.5-2 gm
    3. 5-10 gm
    4. 15-20 gm
(Ref. 1, p. 319)
  1. The normal range of plasma ammonia is:
    1. 10-20 μg/dl
    2. 20-40 μg/dl
    3. 40-80 μg/dl
    4. 1-2 mg/dl
(Ref. 1, p. 317)
  1. Inborn errors of urea cycle can cause all the following except:
    1. Vomiting
    2. Ataxia
    3. Renal failure
    4. Mental retardation
(Ref. 1, p. 321)
  1. Hyperammonaemia type I results from congenital absence of:
    1. Glutamate dehydrogenase
    2. Carbamoyl phosphate synthetase
    3. Ornithine transcarbamoylase
    4. None of the above
(Ref. 1, p. 321)
33 B
34 B
35 D
36 D
37 A
38 C
39 B
212
  1. Congenital absence of ornithine transcarbamoylase causes:
    1. Hyperammonaemia type I
    2. Hyperammonaemia type II
    3. Hyperornithinaemia
    4. Citrullinaemia
(Ref. 1, p. 321)
  1. Congenital deficiency of argininosuccinic acid synthetase leads to:
    1. Argininosuccinic acidaemia
    2. Argininosuccinic aciduria
    3. Citrullinaemia
    4. None of the above
(Ref. 1, p. 321)
  1. Increased excretion of argininosuccinic acid in urine occurs in deficiency of:
    1. Argininosuccinic acid synthetase
    2. Argininosuccinase
    3. Arginase
    4. Ornithine transcarbamoylase
(Ref. 1, p. 321)
  1. All the following are glycogenic amino acids except:
    1. Glycine
    2. Alanine
    3. Leucine
    4. Valine
(Ref. 1, p. 324)
  1. A ketogenic amino acid among the following is:
    1. Leucine
    2. Serine
    3. Threonine
    4. Proline
(Ref. 1, p. 324)
  1. Carbon skeleton of the following amino acid can form glucose as well as fatty acids:
    1. Phenylalanine
    2. Tyrosine
    3. Tryptophan
    4. All of the above
(Ref. 1, p. 324)
  1. Carbon skeleton of the following amino acid can serve as a substrate for gluconeogenesis:
    1. Cysteine
    2. Aspartate
    3. Glutamate
    4. All of the above
(Ref. 1, p. 324)
40 B
41 C
42 B
43 C
44 A
45 D
46 D
213
  1. Ornithine, an intermediate of urea cycle, can also be converted into:
    1. Glutamate
    2. Aspartate
    3. Lysine
    4. Histidine
(Ref. 1, p. 326)
  1. N-Formiminoglutamate is a metabolite of:
    1. Glutamate
    2. Histidine
    3. Tryptophan
    4. Methionine
(Ref. 1, p. 327)
  1. A donor of labile methyl groups is:
    1. Methionine
    2. S-Adenosylmethionine
    3. Methylmalonyl CoA
    4. All of the above
(Ref. 1, p. 339)
  1. Methylmalonyl CoA is a metabolite of:
    1. Valine
    2. Leucine
    3. Isoleucine
    4. All of the above
(Ref. 1, pp. 343-345)
  1. Homogentisic acid is formed from:
    1. Homoserine
    2. Homocysteine
    3. Tyrosine
    4. Tryptophan
(Ref. 1, p. 333)
  1. N-Formylkynurenine is formed from:
    1. Phenylalanine
    2. Tyrosine
    3. Tryptophan
    4. Glutamate
(Ref. 1, pp. 327, 332)
  1. Glyoxylate is formed from:
    1. Glycine
    2. Hydroxyproline
    3. Both of the above
    4. Neither of the above
(Ref. 1, pp. 340, 342)
  1. Maple syrup urine disease results from absence or severe deficiency of:
    1. Homogentisate oxidase
    2. Phenylalanine hydroxylase
    3. Branched-chain amino acid transaminase
    4. None of the above
(Ref. 1, p. 342)
47 A
48 B
49 B
50 A
51 C
52 C
54 D
214
  1. Maple syrup urine disease is an inborn error of metabolism of:
    1. Sulphur-containing amino acids
    2. Aromatic amino acids
    3. Branched-chain amino acids
    4. Dicarboxylic amino acids
(Ref. 1, p. 342)
  1. Urinary excretion of branched-chain α-keto acids is increased in:
    1. Maple syrup urine disease
    2. Intermittent branched-chain ketonuria
    3. Both of the above
    4. Neither of the above
(Ref. 1, pp. 342-343)
  1. Cystinuria results from inability to:
    1. Metabolise cysteine
    2. Convert cystine into cysteine
    3. Incorporate cysteine into proteins
    4. Reabsorb cystine in renal tubules
(Ref. 1, p. 328)
  1. All the following statements about cystinuria are correct except:
    1. Catabolism of cysteine is impaired in this disease
    2. Renal tubular reabsorption of cystine is impaired in it
    3. Renal tubular reabsorption of lysine, arginine and ornithine is also impaired in it
    4. It can lead to the formation of cystine stones in kidneys
(Ref. 1, p. 328)
  1. All of the following statements about homocystinuria are correct except:
    1. The metabolic defect involves cystathionine synthetase
    2. Urinary excretion of homocysteine and homocystine is increased
    3. Plasma methionine level is increased
    4. It can be controlled by giving high-methionine, low-cysteine diet
(Ref. 1, p. 330)
55 C
56 C
57 D
58 A
59 D
215
  1. The defective enzyme in histidinaemia is:
    1. Histidine carboxylase
    2. Histidine decarboxylase
    3. Histidase
    4. Histidine oxidase
(Ref. 1, p. 326)
  1. Phenylketonuria results from absence of:
    1. Phenylalanine transaminase
    2. Phenylalanine hydroxylase
    3. Tyrosinase
    4. Tyrosine transaminase
(Ref. 1, p. 335)
  1. All the following satements about phenylketonuria are correct except:
    1. Phenylalanine cannot be converted into tyrosine
    2. Urinary excretion of phenylpyruvate and phenyl-lactate is increased
    3. It can be controlled by giving a low-phenylalanine diet
    4. It leads to decreased synthesis of thyroid hormones
(Ref. 1, pp. 334-335)
  1. All the following statements about albinism are correct except:
    1. Tyrosine hydroxylase (tyrosinase) is absent or deficient in melanocytes
    2. Skin is hypopigmented
    3. It results in mental retardation
    4. Eyes are hypopigmented
(Ref. 1, p. 354)
  1. All the following features are present in alkaptonuria except:
    1. Absence of homogentisate oxidase
    2. Urine darkens on exposure to air
    3. Pigmentation of connective tissue
    4. Increased conversion of tyrosine into melanin
(Ref. 1, p. 332)
60 C
61 B
62 D
63 C
64 D
216
  1. Glycine is required for the formation of all of the following except:
    1. Porphyrins
    2. Creatine
    3. Glutathione
    4. Pyrimidines
(Ref. 1, pp. 38, 357, 362, 393)
  1. Glycine is not required for the formation of:
    1. Taurocholic acid
    2. Creatine
    3. Purines
    4. Porphyrins
(Ref. 1, pp. 347, 354, 362)
  1. All the following are required for the formation of creatine except:
    1. Creatine kinase
    2. Arginine
    3. S-Adenosylmethionine
    4. Glycine
(Ref. 1, p. 357)
  1. Histamine is formed from histidine by:
    1. Deamination
    2. Dehydrogenation
    3. Decarboxylation
    4. Carboxylation
(Ref. 1, p. 349)
  1. DOPA is an intermediate in the synthesis of:
    1. Thyroid hormones
    2. Catecholamines
    3. Melanin
    4. Catecholamines and melanin
(Ref. 1, pp. 355, 356, 562)
  1. All the following can be formed from tryptophan except:
    1. Niacin
    2. Serotonin
    3. Melatonin
    4. Melanin
(Ref. 1, pp. 353, 354, 630)
  1. All the following statements about pepsin are correct except:
    1. It is smaller than pepsinogen
    2. It is formed by the action of HCl on its precursor
    3. Its optimum pH is 1.0-2.0
    4. It hydrolyses the C-terminal and N-terminal peptide bonds of proteins
(Ref. 1, pp. 663, 668)
65 D
66 A
67 A
68 C
69 D
70 D
71 D
217
  1. Pancreatic juice contains the precursors of all of the following except:
    1. Trypsin
    2. Chymotrypsin
    3. Carboxypeptidase
    4. Aminopeptidase
(Ref. 1, pp. 664-665)
  1. All the following statements about trypsin are true except:
    1. Its precursor is secreted by exocrine portion of pancreas
    2. It is formed by the action of enterokinase on trypsinogen
    3. Active trypsin can also act on its own precursor to form more trypsin
    4. It acts preferentially on peptide bonds involving aromatic amino acids
(Ref. 1, p. 664)
  1. The only correct statement about chymotrypsin is:
    1. It is formed from trypsin
    2. Carboxypeptidase converts trypsin into chymotrypsin
    3. It is a serine protease
    4. It hydrolyses peptide bonds involving basic amino acids
(Ref. 1, pp. 104, 664)
  1. All the following statements about carboxypeptidase are true except:
    1. Its precursor is procarboxypeptidase
    2. Its precursor is present in succus entericus
    3. It is an exopeptidase
    4. It is formed by the action of trypsin on procarboxypeptidase
(Ref. 1, p. 664)
  1. Some amino acids are considered as non-essential for man because:
    1. They are not required for protein synthesis
    2. They do not form any biologically important compound
    3. They can be synthesised in the body
    4. They are formed from essential amino acids
(Ref. 1, p. 307)
72 D
73 D
74 C
75 B
76 C
218
  1. Some amino acids are considered as essential for man because:
    1. They can not be synthesised in the human body
    2. They can form other, non-essential amino acids
    3. Besides proteins, they form other specialised compounds
    4. Their half-lives are very long
(Ref. 1, p. 307)
  1. A low-phenylalanine diet is recommended in:
    1. Phenylketonuria
    2. Alkaptonuria
    3. Maple syrup urine disease
    4. Hartnup's disease
(Ref. 1. p. 335)
  1. All the following statements about transamination are correct except:
    1. The reaction is reversible
    2. It requires pyridoxal phosphate as a coenzyme
    3. All amino acids can undergo transamination
    4. A Schiff base is formed as an intermediate during the reaction
(Ref. 1, p. 315)
  1. All the following statements about ornithine are correct except:
    1. It is formed during creatine synthesis
    2. It is formed during synthesis of nitric oxide from arginine
    3. It is formed as an intermediate in urea cycle
    4. It can form polyamines
(Ref. 1, pp. 320, 349, 357)
  1. All the following statements about branched-chain amino acids are correct except:
    1. They are essential amino acids
    2. They are transaminated by a common enzyme
    3. They are glucogenic
    4. Their catabolism is impaired in maple syrup urine disease
(Ref. 1, pp. 307, 340, 342)
77 A
78 A
79 C
80 B
81 C
219
  1. Tetrahydrobiopterin is required for hydroxylation of:
    1. Phenylalanine
    2. Tyrosine
    3. Tryptophan
    4. All of the above
(Ref. 1, pp. 311, 352, 588)
  1. N-Acetylglutamate is:
    1. A metabolite of glutamine
    2. An inhibitor of cytosolic carbamoyl phosphate synthetase
    3. An activator of mitochondrial carbamoyl phosphate synthetase
    4. All of the above
(Ref. 1, p. 319)
  1. Cysteine is required to synthesise:
    1. Taurine
    2. CoA
    3. Glutathione
    4. All of the above
(Ref. 1, pp. 38, 349)
  1. Histidine is:
    1. Decarboxylated to urocanic acid
    2. Deaminated to histamine
    3. A semi-essential amino acid
    4. All of the above
(Ref. 1, pp. 307, 327, 349)
  1. Daily degradation of proteins in human adults is about:
    1. 1 -2 % of total body proteins
    2. 5-10 % of total body proteins
    3. 25 - 50% of total body proteins
    4. 75-100% of total body proteins
(Ref. 1, p. 313)
  1. The only fate of amino acids liberated from hydrolysis of body proteins is:
    1. Synthesis of glucose and / or fatty acids
    2. Reutilisation for synthesis of proteins
    3. Catabolism
    4. None of the above
(Ref. 1, p. 313)
82 D
83 C
84 D
85 C
86 A
87 D
220
  1. Asialoglycoproteins are:
    1. Glycoproteins from which sialic acid moiety has been removed
    2. Recognised by specific receptors on liver cells
    3. Hydrolysed in liver cell lysosomes
    4. All of the above
(Ref. 1, p. 314)
  1. Vitamin C is required for hydroxylation of:
    1. Phenylalanine
    2. Tyrosine
    3. Dopamine
    4. All of the above
(Ref. 1, pp. 311, 356)
  1. Inhibitors of mono amine oxidase prolong the life of:
    1. Serotonin
    2. Epinephrine
    3. Dopamine
    4. All of the above
(Ref. 1, pp. 352, 591)
  1. All the following can be formed from serine except:
    1. Threonine
    2. Glycine
    3. Pyruvate
    4. Sphingosine
(Ref. 1, pp. 264, 327)
  1. Vitamin C is required for the synthesis of:
    1. Hydroxyproline
    2. Hydroxylysine
    3. Norepinephrine
    4. All of the above
(Ref. 1, pp. 311, 356)
  1. An amino acid that can not undergo transamination is:
    1. Lysine
    2. Phenylalanine
    3. Tyrosine
    4. None of the above
(Ref. 1, pp. 334-335)
  1. Urinary excretion of homogentisic acid is increased in:
    1. Tyrosinaemia
    2. Alkaptonuria
    3. Phenylketonuria
    4. Homocystinuria
(Ref. 1, pp. 330, 332, 335)
88 D
89 C
90 D
91 A
92 D
93 A
94 B
221
  1. Tetrahydrobiopterin is required for the hydroxylation of:
    1. Phenylalanine
    2. Proline residues
    3. Lysine residues
    4. All of the above
(Ref. 1, p. 311)
  1. All the following statements about ubiquitin are true except:
    1. It is an intracellular protein in eukaryotes
    2. It binds proteins to target them for hydrolysis
    3. Its C-terminal amino acid forms a peptide bond with N-terminal amino acid of the protein to be hydrolysed
    4. Binding of ubiquitin to proteins is ATP-dependent
(Ref. 1, p.314)
  1. The only correct statement about transamination is:
    1. All amino acids can undergo transamination
    2. Only the α-amino groups of amino acids can undergo transamination
    3. Removal of amino group always converts the amino acid into a keto acid
    4. No energy is spent/released during transamination
(Ref. 1, pp. 315-325)
  1. Branched-chain amino acids are used mainly in:
    1. Liver
    2. Muscles
    3. Kidneys
    4. Intestine
(Ref. 1, pp. 318-319)
  1. Primary hyperoxaluria results from a defect in:
    1. Tubular reabsorption of glyoxylate
    2. Catabolism of hydroxyproline
    3. Catabolism of glyoxylate
    4. Intestinal absorption of oxalate
(Ref. 1, p. 327)
  1. One-carbon unit is liberated during catabolism of:
    1. Histidine
    2. Serine
    3. Glycine
    4. All of the above
(Ref. 1, pp. 327-328)
95 A
96 C
97 D
98 B
99 C
100 D

Immunochemistry18

  1. The portion of the antigen molecule which is recognised by antibody is known as:
    1. Hapten
    2. Epitope
    3. Complement
    4. Variable region
(Ref. 1, p. 746)
  1. All the following statements about haptens are true except:
    1. They have high molecular weights
    2. They cannot elicit an immune response by themselves
    3. When combined with some other large molecule, they can elicit an immune response
    4. Once an immune response develops, the free hapten can be recognised by the antibody
(Ref. 1, pp. 784-785)
  1. Antigens and haptens have the following similarity:
    1. They have high molecular weights
    2. They can elicit immune response by themselves
    3. They can elicit an immune response only in association with some other large molecule
    4. Once an immune response develops, free antigen and free hapten can be recognised by the antibody.
(Ref. 2, p. 362)
  1. The minimum number of polypeptide chains in an immunoglobulin is:
    1. Two
    2. Four
    3. Five
    4. Six
(Ref. 1, p. 746)
1 B
2 A
3 D
4 B
223
  1. Light chains of immunoglobulins are of following types:
    1. Alpha and kappa
    2. Alpha and gamma
    3. Lambda and delta
    4. Kappa and lambda
(Ref. 1, p. 746)
  1. Immunoglobulins are classified on the basis of:
    1. Type of light chains
    2. Type of heavy chains
    3. Types of light and heavy chains
    4. Molecular weight
(Ref. 1, p. 747)
  1. The molecular weight of light chains is:
    1. 15,000
    2. 23,000
    3. 50,000
    4. 70,000
(Ref. 1, p. 746)
  1. The molecular weight of heavy chains is:
    1. 15,000-23,000
    2. 24,000-52,000
    3. 53,000-75,000
    4. 76,000-100,000
(Ref. 1, p. 746)
  1. Secretory component is present in:
    1. IgA
    2. IgG
    3. IgM
    4. All of the above
(Ref. 1, p. 749)
  1. The variable region of light chains is the:
    1. N-terminal quarter
    2. N-terminal half
    3. C-terminal quarter
    4. C-terminal half
(Ref. 1, p. 746)
  1. The variable region of heavy chains is the:
    1. N-terminal quarter
    2. N-terminal half
    3. C-terminal quarter
    4. C-terminal half
(Ref. 1, p. 746)
  1. The variable region of light chains has:
    1. One hypervariable region
    2. Two hypervariable regions
    3. Three hypervariable regions
    4. Four hypervariable regions
(Ref. 1, p. 747)
5 D
6 B
7 B
8 C
9 A
10 B
11 A
12 C
224
  1. The variable region of heavy chains has:
    1. One hypervariable region
    2. Two hypervariable regions
    3. Three hypervariable regions
    4. Four hypervariable regions
(Ref. 1, p. 747)
  1. The most abundant immunoglobulin in plasma is:
    1. IgA
    2. IgG
    3. IgM
    4. IgD
(Ref. 1, p. 748)
  1. The largest immunoglobulin is:
    1. IgA
    2. IgG
    3. IgM
    4. IgD
(Ref. 1, p. 748)
  1. The plasma concentration of IgA is:
    1. 1-5 mg/dl
    2. 40-200 mg/dl
    3. 60-500 mg/dl
    4. D. 700-1,500 mg/dl
(Ref. 2, p. 375)
  1. An immunoglobulin found in exocrine secretions is:
    1. IgA
    2. IgG
    3. IgM
    4. IgE
(Ref. 2, p. 375)
  1. Allergic reactions are mediated by:
    1. IgA
    2. IgG
    3. IgD
    4. IgE
(Ref. 2, p. 376)
  1. An immunoglobulin which can cross the placental barrier is:
    1. IgA
    2. IgM
    3. IgD
    4. None of the above
(Ref. 1, p. 748)
  1. IgM possesses:
    1. Two light chains and two heavy chains
    2. Four light chains and four heavy chains
    3. Six light chains and six heavy chains
    4. Ten light chains and ten heavy chains
(Ref. 1, p. 749)
  1. The immunoglobulin having the longest half-life is:
    1. IgA
    2. IgG
    3. IgM
    4. IgE
(Ref. 6, p. 338)
13 D
14 B
15 C
16 C
17 A
18 D
19 D
20 D
21 B
225
  1. The half-life of IgG is:
    1. 2-3 days
    2. 5-6 days
    3. 8-10 days
    4. 20-25 days
(Ref. 6, p. 338)
  1. Recognition of antigen is the function of:
    1. Variable region of light chains
    2. Variable regions of light and heavy chains
    3. Constant region of heavy chains
    4. Constant regions of light and heavy chains
(Ref. 1, p. 456)
  1. The effector function of antibody is performed by:
    1. Variable region of heavy chains
    2. Constant region of heavy chains
    3. Variable regions of light and heavy chains
    4. Constant regions of light and heavy chains
(Ref. 1, p. 749)
  1. Complement system can be activated by binding of antigen to:
    1. IgA
    2. IgD
    3. IgE
    4. IgM
(Ref. 2, p. 376)
  1. C1 component of classical complement pathway is made up of:
    1. Complements 1q and 1r
    2. Complements 1q and 1s
    3. Complements 1r and 1s
    4. Complements 1q, 1r and 1s
(Ref. 2, p. 376)
  1. The components of complement system are activated by:
    1. Microsomal hydroxylation
    2. Phosphorylation
    3. Glycosylation
    4. Proteloysis
(Ref. 1, p. 751)
  1. The complement system forms a membrane attack complex made up of:
    1. Complements 1q, 1r and 1s
    2. Complements 1, 2, 3 and 4
    3. Complements 5,6,7,8 and 9
    4. Factors B and D
(Ref. 1, p. 751)
22 D
23 B
24 D
25 D
26 D
27 D
28 C
226
  1. Factors B and D are required in:
    1. The classical pathway of complement fixation
    2. The alternate complement pathway
    3. Both of the above
    4. Neither of the above
(Ref. 6, p. 342)
  1. The alternate complement pathway doesn't involve:
    1. Antigen-antibody complex
    2. Complement 3
    3. Factors B and D
    4. Membrane attack unit
(Ref. 6, p. 342)
  1. Antibody diversity arises from:
    1. Gene amplification
    2. Gene re-arrangement
    3. Alternative splicing
    4. All of the above
(Ref. 1, p. 485)
  1. A light chain gene is constructed from the following segments:
    1. Variable and constant segments
    2. Variable, joining and constant segments
    3. Variable, diversity and constant segments
    4. Variable, joining, diversity and constant segments
(Ref. 1, p. 485)
  1. A heavy chain gene is constructed from the following segments:
    1. Variable and constant segments
    2. Variable, joining and constant segments
    3. Variable, diversity and constant segments
    4. Variable, joining, diversity and constant segments
(Ref. 1, p. 485)
  1. Diversity segments are present in:
    1. Light chain genes
    2. Heavy chain genes
    3. Light and heavy chain genes
    4. None of the above
(Ref. 1, p. 485)
  1. Constant segments of heavy chains are of:
    1. Five types
    2. Six types
    3. Seven types
    4. Eight types
(Ref. 2, p. 377)
29 B
30 A
31 B
32 B
33 D
34 B
35 D
227
  1. Gamma heavy chains are of:
    1. Two types
    2. Three types
    3. Four types
    4. Five types
(Ref. 1, p. 748)
  1. Gamma heavy chains are present in:
    1. IgA
    2. IgG
    3. IgM
    4. IgD
(Ref. 1, p. 485)
  1. Heavy chains in IgD are of following type:
    1. Alpha
    2. Gamma
    3. Delta
    4. Epsilon
(Ref. 1, p. 748)
  1. On exposure to any antigen, the first antibody to be formed is of the following class:
    1. IgA
    2. IgG
    3. IgM
    4. IgE
(Ref. 2, p. 377)
  1. Constant segment genes of heavy chains are present in a cluster in which the first gene on 5' side is:
    1. Alpha
    2. Gamma
    3. Delta
    4. None of the above
(Ref. 2, p. 377)
  1. Cell-mediated immunity is the function of:
    1. B lymphocytes
    2. T lymphocytes
    3. Plasma cells
    4. Basophils
(Ref. 1, p. 746)
  1. The most abundant T cells are:
    1. Cytotoxic T cells
    2. Helper T cells
    3. Suppressor T cells
    4. Memory T cells
(Ref. 2, pp. 378-379)
  1. T cells can recognise:
    1. Free antigens
    2. Antigens bound to cells
    3. Antigens bound to antibodies
    4. Antigens bound to MHC proteins
(Ref. 2, p. 387)
  1. MHC proteins are unique to:
    1. Each cell
    2. Each organ
    3. Each individual
    4. Each species
(Ref. 2, p. 380)
36 C
37 B
38 C
39 C
40 D
41 B
42 B
43 D
44 C
228
  1. MHC Class I proteins are present on the surface of:
    1. B cells only
    2. T cells only
    3. Macrophages only
    4. All cells
(Ref. 6, p. 346)
  1. MHC Class I proteins, in conjunction with antigens, are recognised by:
    1. Cytotoxic T cells
    2. Helper T cells
    3. Suppressor T cells
    4. Memory T cells
(Ref. 2, p. 379)
  1. MHC Class II proteins are present on the surface of:
    1. All cells
    2. B lymphocytes only
    3. Macrophages only
    4. Macrophages and B lymphocytes
(Ref. 2, p. 379)
  1. MHC Class II proteins, in conjunction with antigens, are recognised by:
    1. Cytotoxic T cells
    2. Helper T cells
    3. Suppressor T cells
    4. Memory T cells
(Ref. 2, p. 379)
  1. CD 8 is a transmembrane glycoprotein present in:
    1. Cytotoxic T cells
    2. Helper T cells
    3. Suppressor T cells
    4. Memory T cells
(Ref. 2, p. 384)
  1. CD 4 is a transmembrane glycoprotein present in:
    1. Cytotoxic T cells
    2. Helper T cells
    3. Suppressor T cells
    4. Memory T cells
(Ref. 2, p. 384)
  1. CD 3 complex and p 56lck proteins are present in:
    1. Cytotoxic T cells
    2. Helper T cells
    3. Both of the above
    4. Neither of the above
(Ref. 2, pp. 383-384)
  1. Cytotoxic T cells release:
    1. Perforins
    2. Interleukins
    3. Colony stimulating factors
    4. Tumour necrosis factor
(Ref. 2, p. 384)
45 D
46 A
47 D
48 B
49 A
50 B
51 C
52 A
229
  1. Helper T cells release:
    1. Interleukins
    2. Colony stimulating factors
    3. Tumour necrosis factor
    4. All of the above
(Ref. 6, p. 347)
  1. MHC Class III proteins include:
    1. Immunoglobulins
    2. Components of complement system
    3. T cell receptors
    4. CD4 and CD8 proteins
(Ref. 3, p. 380)
  1. Human immunodeficiency virus destroys:
    1. Cytotoxic T cells
    2. Helper T cells
    3. B cells
    4. Plasma cells
(Ref. 2, p. 385)
  1. In allergic diseases, the concentration of the following is increased in plasma:
    1. IgA
    2. IgG
    3. IgD
    4. IgE
(Ref. 6, p. 339)
  1. IgE has a tendency to attach to:
    1. Basophils
    2. Mast cells
    3. Both of the above
    4. Neither of the above
(Ref. 6, p. 338)
  1. An antibody that defends against worm infections is:
    1. IgA
    2. IgG
    3. IgD
    4. IgE
(Ref. 1, p. 748)
  1. Active immunity can be produced by administration of:
    1. Killed bacteria or viruses
    2. Live attenuated bacteria or viruses
    3. Toxoids
    4. All of the above
(Ref. 6, p. 335)
  1. Passive immunity can be produced by administration of:
    1. Pure antigens
    2. Immunoglobulins
    3. Toxoids
    4. Killed bacteria or viruses
(Ref. 6, p. 335)
53 D
54 B
55 B
56 D
57 C
58 D
59 D
60 B
230
  1. Helper T cells release all the following except:
    1. Interleukins
    2. Colony stimulating factors
    3. Perforins
    4. Tumour necrosis factors
(Ref. 6, p. 347)
  1. IgG is cleaved by papain into:
    1. Two light and two heavy chains
    2. Two Fab and one Fc fragments
    3. Two pairs of one light and one heavy chain each
    4. One Fab and two Fc fragments
(Ref. 1, p. 746)
  1. Bence-Jones protein is:
    1. An immunoglobulin
    2. A dimer of heavy chains
    3. A dimer of light chains
    4. A dimer of one heavy and one light chains
(Ref. 2, p. 368)
  1. Bence-Jones proteins possess all the following properties except:
    1. They are dimers of light chains
    2. Their amino acid sequences are identical
    3. Their N-terminal halves have variable amino acid sequences
    4. Their C-terminal halves have constant amino acid sequences
(Ref. 2, p. 368)
  1. Variable regions are present in:
    1. Immunoglobulins
    2. α-Chains of T cell receptors
    3. β-Chains of T cell receptors
    4. All of the above
(Ref. 2, pp. 382-383)
  1. Immunoglobulins are secreted by:
    1. B lymphocytes
    2. Plasma cells
    3. Thymus cells
    4. T lymphocytes
(Ref. 1, p. 746)
61 C
62 B
63 C
64 B
65 D
66 B
231
  1. Cell-mediated immunity is the function of:
    1. B lymphocytes
    2. Plasma cells
    3. Bone marrow cells
    4. T lymphocytes
(Ref. 1, p. 746)
  1. T lymphocytes are processed in:
    1. Thyroid gland
    2. Thymus
    3. Thalamus
    4. Bone marrow
(Ref. 1, p. 746)
  1. Plasma cells specialise from:
    1. T lymphocytes
    2. B lymphocytes
    3. Macrophages
    4. Erythrocytes
(Ref. 1, p. 746)
  1. Papain cleaves an immunoglobulin molecule:
    1. Between CH1 and CH2 domains
    2. Between CH2 and CH3 domains
    3. Between VH and CH1 domains
    4. Into light and heavy chains
(Ref. 1, p. 746)
  1. Monoclonal antibodies are prepared by cloning:
    1. Myeloma cells
    2. Hybridoma cells
    3. T lymphocytes
    4. B lymphocytes
(Ref. 1, pp. 750-751)
  1. Myeloma cells are lacking in:
    1. TMP synthetase
    2. Formyl transferase
    3. HGPRT
    4. All of the above
(Ref. 1, p. 751)
  1. Hybridoma cells are selected by culturing them in a medium containing:
    1. Adenine, guanine, cytosine and thymine
    2. Adenine, guanine, cytosine and uracil
    3. Hypoxanthine, aminopterin and thymine
    4. Hypoxanthine, aminopterin and thymidine
(Ref. 1, pp. 750-751)
  1. Myeloma cells and lymphocytes can be fused by using:
    1. Calcium chloride
    2. Ethidium bromide
    3. Polyethylene glycol
    4. DNA polymerase
(Ref. 1, p. 750)
67 D
68 B
69 B
70 A
71 B
72 C
73 D
74 C

Minerals19

  1. The total amount of calcium in an average adult man is about:
    1. 100 gm
    2. 500 gm
    3. 1 kg
    4. 10 kg
(Ref. 1, p. 567)
  1. The following proportion of the total body calcium is present in bones and teeth:
    1. 75%
    2. 90%
    3. 95%
    4. 99%
(Ref. 1, p. 567)
  1. The normal range of plasma calcium is:
    1. 3-5 mg/dl
    2. 5-10 mg/dl
    3. 9-11 mg/dl
    4. 11-15 mg/dl
(Ref. 6, p. 429)
  1. The normal range of ionised calcium in plasma is:
    1. 2-4 mg/dl
    2. 2-4 mEq/L
    3. 4-5mg/dl
    4. 4-5mEq/L
(Ref. 6, p. 429)
  1. Tetany can occur in:
    1. Hypocalcaemia
    2. Hypercalcaemia
    3. Alkalosis
    4. Hypocalcaemia and alkalosis
(Ref. 6, p. 431)
  1. Intestinal absorption of calcium occurs by:
    1. Active uptake
    2. Simple diffusion
    3. Facilitated diffusion
    4. Endocytosis
(Ref. 1, p. 571)
1 C
2 D
3 C
4 C
5 D
6 A
233
  1. Intestinal absorption of calcium is hampered by:
    1. Phosphate
    2. Phytate
    3. Proteins
    4. Lactose
(Ref. 3, p. 779)
  1. Calcitriol facilitates calcium absorption by increasing the synthesis of the following in intestinal mucosa:
    1. Calcium-binding protein
    2. Alkaline phosphatase
    3. Calcium-dependent ATPase
    4. All of the above
(Ref. 5, p. 192)
  1. A high plasma calcium level decreases intestinal absorption of calcium by:
    1. Stimulating the secretion of parathormone
    2. Inhibiting the secretion of parathormone
    3. Decreasing the synthesis of cholecalciferol
    4. Inhibiting the secretion of thyrocalcitonin
(Ref. 1, pp. 570, 573)
  1. The daily calcium requirement of an adult man is about:
    1. 400 mg
    2. 600 mg
    3. 800 mg
    4. 1,000 mg
(Ref. 1, p. 660)
  1. The daily calcium requirement in pregnancy and lactation is about:
    1. 600 mg
    2. 800 mg
    3. 1,200 mg
    4. 1,500 mg
(Ref. 1, p. 660)
  1. Hypercalcaemia can occur in all the following except:
    1. Hyperparathyroidism
    2. Hypervitaminosis D
    3. Milk alkali syndrome
    4. Nephrotic syndrome
(Ref. 5, pp. 819-820)
  1. Hypocalcaemia can occur in all the following except:
    1. Rickets
    2. Osteomalacia
    3. Hyperparathyroidism
    4. Intestinal malabsorption
(Ref. 5, p. 820)
7 B
8 D
9 B
10 C
11 C
12 D
13 C
234
  1. The major calcium salt in bones is:
    1. Calcium carbonate
    2. Calcium chloride
    3. Calcium hydroxide
    4. Calcium phosphate
(Ref. 1, p. 567)
  1. The correct statement about serum inorganic phosphorus concentration is:
    1. It is higher in men than in women
    2. It is higher in women than in men
    3. It is higher in adults than in children
    4. It is higher in children than in adults
(Ref. 6, p. 432)
  1. The product of serum calcium concentration (mg/dl) and serum inorganic phosphorus concentration (mg/dl) in adults is about:
    1. 30
    2. 40
    3. 50
    4. 60
(Ref. 6, p. 431)
  1. The product of serum calcium concentration (mg/dl) and serum inorganic phosphorus concentration (mg/dl) in children is about:
    1. 30
    2. 40
    3. 50
    4. 60
(Ref. 6, p. 431)
  1. The product of serum calcium concentration (mg/dl) and serum inorganic phosphorus concentration (mg/dl) is decreased in:
    1. Rickets
    2. Hypoparathyroidism
    3. Hyperparathyroidism
    4. Renal failure
(Ref. 5, p. 821)
  1. Serum inorganic phosphorus rises in all the following conditions except:
    1. Hypoparathyroidism
    2. Hypervitaminosis D
    3. Chronic renal failure
    4. After a carbohydrate-rich meal
(Ref. 5, p. 821)
14 D
15 D
16 B
17 C
18 A
19 D
235
  1. Serum inorganic phosphorus decreases in all the following conditions except:
    1. Hyperparathyroidism
    2. Intestinal malabsorption
    3. Osteomalacia
    4. Chronic renal failure
(Ref. 5, p. 821)
  1. Serum magnesium level ranges between:
    1. 2-3 mg/dl
    2. 3-5 mg/dl
    3. 6-8 mg/dl
    4. 9-11 mg/dl
(Ref. 1, p. 869)
  1. Magnesium ions are required in the reactions involving:
    1. NAD
    2. FAD
    3. ATP
    4. CoA
(Ref. 3, p. 779)
  1. Normal range of serum sodium is:
    1. 30-70 mEq/L
    2. 70-110 mEq/L
    3. 117-135 mEq/L
    4. 136-145 mEq/L
(Ref. 1, p. 870)
  1. Sodium is involved in the active uptake of:
    1. D-Glucose
    2. D-Galactose
    3. L-Amino acids
    4. All of the above
(Ref. 1, pp. 667, 670)
  1. Aldosterone increases reabsorption of sodium in:
    1. Proximal convoluted tubules
    2. Ascending limb of loop of Henle
    3. Descending limb of loop of Henle
    4. Distal convoluted tubules
(Ref. 1, p. 582)
  1. Restriction of sodium intake is commonly advised in:
    1. Addison's disease
    2. Diarrhoea
    3. Hypertension
    4. None of the above
(Ref. 3, p. 780)
20 D
21 A
22 C
23 D
24 D
25 D
26 C
236
  1. Serum sodium level rises in all of the following except:
    1. Renal failure
    2. Prolonged steroid therapy
    3. Aldosteronism
    4. Dehydration
(Ref. 6, p. 433)
  1. Hyponatraemia occurs in the following condition:
    1. Addison's disease
    2. Chronic renal failure
    3. Severe diarrhoea
    4. All of the above
(Ref. 5, pp. 768-769, 814-815)
  1. Serum potassium level decreases in:
    1. Familial periodic paralysis
    2. Addison's disease
    3. Renal failure
    4. All of the above
(Ref. 5, pp. 768-769, 816-817)
  1. Concentration of the following is higher in intracellular fluid than in extracellular fluid:
    1. Sodium
    2. Potassium
    3. Chloride
    4. D Bicarbonate
(Ref. 3, p. 705)
  1. Normal range of serum potassium is:
    1. 2.1-3.4 mEq/L
    2. 3.5-5.3 mEq/L
    3. 5.4-7.4 mEq/L
    4. 7.5-9.5 mEq/L
(Ref. 1, p. 870)
  1. Normal range of serum chloride is:
    1. 24-27 mEq/L
    2. 70-80 mEq/L
    3. 100-106 mEq/L
    4. 120-140 mEq/L
(Ref. 1, p. 869)
  1. An extracellular fluid having a higher concentration of chloride than serum is:
    1. Bile
    2. Sweat
    3. CSF
    4. Pancreatic juice
(Ref. 6, p. 434)
27 A
28 D
29 A
30 B
31 B
32 C
33 C
237
  1. Total amount of iron in an adult man is about:
    1. 1-2 gm
    2. 2-3 gm
    3. 3-4 gm
    4. 6-7 gm
(Ref. 1, p. 742)
  1. Haemoglobin contains about:
    1. 30% of the total body iron
    2. 50% of the total body iron
    3. 75% of the total body iron
    4. 90% of the total body iron
(Ref. 6, p. 435)
  1. About 5% of the total body iron is present in:
    1. Transferrin
    2. Myoglobin
    3. Cytochromes
    4. Haemosiderin
(Ref. 6, p. 435)
  1. Each haemoglobin molecule contains:
    1. One iron atom
    2. Two iron atoms
    3. Four iron atoms
    4. Six iron atoms
(Ref. 6, p. 366)
  1. Each myoglobin molecule contains:
    1. One iron atom
    2. Two iron atoms
    3. Four iron atoms
    4. Six iron atoms
(Ref. 6, p. 376)
  1. Apoferritin molecule is made up of:
    1. Four subunits
    2. Eight subunits
    3. Ten subunits
    4. Twenty-four subunits
(Ref. 1, p. 742)
  1. Ferritin is present in:
    1. Intestinal mucosa
    2. Liver
    3. Spleen
    4. All of the above
(Ref. 6, p. 437)
  1. Iron is stored in the form of:
    1. Ferritin and transferrin
    2. Transferrin and haemosiderin
    3. Haemoglobin and myoglobin
    4. Ferritin and haemosiderin
(Ref. 3, p. 781)
34 C
35 C
36 B
37 C
38 A
39 D
40 D
41 D
238
  1. Iron is transported in blood in the form of:
    1. Ferritin
    2. Haemosiderin
    3. Transferrin
    4. Haemoglobin
(Ref. 1, p. 741)
  1. Molecular weight of transferrin is about:
    1. 40,000
    2. 60,000
    3. 80,000
    4. 100,000
(Ref. 1, p. 741)
  1. Normal plasma iron level is:
    1. 50-100 εg/dl
    2. 100-150 εg/dl
    3. 50-175 εg/dl
    4. 250-400 ε/dl
(Ref. 1, p. 869)
  1. Iron is present in all of the following except:
    1. Peroxidase
    2. Xanthine oxidase
    3. Aconitase
    4. Fumarase
(Ref. 3, pp. 270, 445, 447, 634)
  1. Total daily iron loss of an adult man is about:
    1. 0.1 mg
    2. 1 mg
    3. 5 mg
    4. 10 mg
(Ref. 1, p. 742)
  1. Iron absorption is hampered by:
    1. Ascorbic acid
    2. Succinic acid
    3. Phytic acid
    4. Amino acid
(Ref. 6, p. 436)
  1. Iron absorption is decreased:
    1. In achlorhydria
    2. When ferritin content of intestinal mucosa is low
    3. When saturation of plasma transferrin is low
    4. When erythropoietic activity is increased
(Ref. 6, p. 438)
  1. Daily iron requirement of an adult man is about:
    1. 1 mg
    2. 5 mg
    3. 10 mg
    4. 18 mg
(Ref. 5, p. 828)
  1. Daily iron requirement of a woman of reproductive age is about:
    1. 1 mg
    2. 2 mg
    3. 10 mg
    4. 20 mg
(Ref. 5, p. 828)
42 C
43 C
44 C
45 D
46 B
47 C
48 A
49 C
50 D
239
  1. All the following are good sources of iron except:
    1. Milk
    2. Meat
    3. Liver
    4. Kidney
(Ref. 3, p. 780)
  1. Relatively more iron is absorbed from:
    1. Green leafy vegetables
    2. Fruits
    3. Whole grain cereals
    4. Organ meats
(Ref. 3, p. 780)
  1. Iron absorption from a mixed diet is about:
    1. 1-5 %
    2. 5-10 %
    3. 20-25 %
    4. 25-50 %
(Ref. 5, p. 827)
  1. Iron deficiency causes:
    1. Normocytic anaemia
    2. Microcytic anaemia
    3. Megaloblastic anaemia
    4. Pernicious anaemia
(Ref. 1, p. 659)
  1. Prolonged and severe iron deficiency can cause atrophy of epithelium of:
    1. Oral cavity
    2. Oesophagus
    3. Stomach
    4. All of the above
(Ref. 6, p. 438)
  1. All the following statements about bronzed diabetes are true except:
    1. It is caused by excessive intake of copper
    2. Skin becomes pigmented
    3. There is damage to β cells of islets of Langerhans
    4. Liver is damaged
(Ref. 1, p. 865)
  1. The total amount of iodine in the body of an average adult is:
    1. 10-15 mg
    2. 20-25 mg
    3. 45-50 mg
    4. 75-100 mg
(Ref. 5, p. 721)
  1. Iodine content of thyroid gland in an adult is about:
    1. 1-3 mg
    2. 4-8 mg
    3. 10-15 mg
    4. 25-30 mg
(Ref. 5, p. 721)
51 A
52 D
53 B
54 B
55 D
56 A
57 C
58 C
240
  1. Daily iodine requirement of an adult is about:
    1. 50 μg
    2. 100 μg
    3. 150 μg
    4. 1 mg
(Ref. 1, p. 660)
  1. Consumption of iodised salt is recommended in:
    1. Patients with hyperthyroidism
    2. Patients with hypothyroidism
    3. Pregnant women
    4. Goitre belt areas
(Ref. 6, p. 439)
  1. All the following statements about endemic goitre are true except:
    1. It occurs in areas where soil and water have low iodine content
    2. It leads to enlargement of thyroid gland
    3. It results ultimately in hyperthyroidism
    4. It can be prevented by consumption of iodised salt
(Ref. 3, pp. 781-782)
  1. The total amount of copper in the body of an average adult is:
    1. 1 gm
    2. 500 mg
    3. 100 mg
    4. 10 mg
(Ref. 6, p. 438)
  1. The normal range of plasma copper is:
    1. 25-50 μg/dl
    2. 50-100 μg/dl
    3. 100-200 μg/dl
    4. 200-400 μg/dl
(Ref. 1, p. 869)
  1. Copper deficiency can cause:
    1. Polycythaemia
    2. Leukocytopenia
    3. Thrombocytopenia
    4. Microcytic anaemia
(Ref. 1, p. 659)
  1. Daily requirement of copper in adults is about:
    1. 0.5 mg
    2. 1 mg
    3. 2.5 mg
    4. 5 mg
(Ref. 5, p. 831)
59 C
60 D
61 C
62 C
63 C
64 D
65 C
241
  1. All the following statements about ceruloplasmin are correct except:
    1. It is a copper-containing protein
    2. It possesses oxidase activity
    3. It is synthesised in intestinal mucosa
    4. Its plasma level is decreased in Wilson's disease
(Ref. 1, p. 743)
  1. All the following statements about Wilson's disease are correct except:
    1. It is a genetic disease
    2. The defect involves copper-dependent P-type ATPase
    3. Copper is deposited in liver, basal ganglia and around cornea
    4. Plasma copper level is increased in it
(Ref. 1, pp. 743-744)
  1. All the following statements about Menkes' disease are true except:
    1. It is an inherited disorder of copper metabolism
    2. It occurs only in males
    3. Plasma copper is increased in it
    4. Hair becomes steely and kinky in it
(Ref. 1, p. 743)
  1. The total amount of zinc in an average adult is:
    1. 0.25-0.5 gm
    2. 0.5-1.0 gm
    3. 1.5-2.0 gm
    4. 2.5-5.0 gm
(Ref. 5, p. 836)
  1. Plasma zinc level is:
    1. 10-50 ε/dl
    2. 50-150 ε/dl
    3. 150-250 εg/dl
    4. 250-500 εg/dl
(Ref. 1, p. 870)
  1. Zinc is a cofactor for:
    1. Acid phosphatase
    2. Alkaline phosphatase
    3. Amylase
    4. Lipase
(Ref. 1, p. 659)
  1. Zinc is involved in storage and release of:
    1. Histamine
    2. Acetylcholine
    3. Epinephrine
    4. Insulin
(Ref. 6, p. 440)
66 C
67 D
68 C
69 C
70 B
71 B
72 D
242
  1. Intestinal absorption of zinc is retarded by:
    1. Calcium
    2. Cadmium
    3. Phytate
    4. All of the above
(Ref. 6, p. 440)
  1. The daily zinc requirement of an average adult is:
    1. 5 mg
    2. 10 mg
    3. 15 mg
    4. 25 mg
(Ref. 1, p. 660)
  1. Zinc deficiency occurs commonly in:
    1. Acrodermatitis enteropathica
    2. Wilson's disease
    3. Xeroderma pigmentosum
    4. Menkes' disease
(Ref. 6, p. 440)
  1. Hypogonadism can occur in deficiency of:
    1. Copper
    2. Chromium
    3. Zinc
    4. Manganese
(Ref. 1, p. 659)
  1. Healing of wounds may be impaired in deficiency of:
    1. Selenium
    2. Copper
    3. Zinc
    4. Cobalt
(Ref. 1, p. 659)
  1. Hypochromic microcytic anaemia can occur in deficiency of:
    1. Zinc
    2. Copper
    3. Manganese
    4. None of the above
(Ref. 1, p. 659)
  1. The daily requirement for manganese in adults is about:
    1. 1-2 mg
    2. 2-5 mg
    3. 2-5 μg
    4. 5-20 μg
(Ref. 1, p. 660)
  1. Molybdenum is a cofactor for:
    1. Xanthine oxidase
    2. Aldehyde oxidase
    3. Sulphite oxidase
    4. All of the above
(Ref. 6, p. 441)
73 D
74 C
75 A
76 C
77 C
78 B
79 B
80 D
243
  1. A trace element having antioxidant function is:
    1. Selenium
    2. Tocopherol
    3. Chromium
    4. Molybdenum
(Ref. 1, p. 659)
  1. Selenium is a constituent of:
    1. Glutathione reductase
    2. Glutathione peroxidase
    3. Catalase
    4. Superoxide dismutase
(Ref. 1, p. 659)
  1. Selenium decreases the requirement of:
    1. Copper
    2. Zinc
    3. Vitamin D
    4. Vitamin E
(Ref. 5, p. 844)
  1. Upper safe limit of fluorine in water is:
    1. 0.4 ppm
    2. 0.8 ppm
    3. 1.2 ppm
    4. 2 ppm
(Ref. 5, p. 835)
  1. The daily fluoride intake should not exceed:
    1. 0.5 mg
    2. 1 mg
    3. 2 mg
    4. 3 mg
(Ref. 5, p. 835)
  1. Calcium is involved in all of the following except:
    1. Formation of bones
    2. Nerve function
    3. Muscle function
    4. Regulation of water balance
(Ref. 1, p. 658)
  1. All the following affect calcium balance except:
    1. Vitamin D
    2. Aldosterone
    3. Parathyroid hormone
    4. Calcitonin
(Ref. 1, p. 658)
  1. Magnesium deficiency can occur in all the following except:
    1. Recurrent vomiting
    2. Chronic diarrhoea
    3. Intestinal malabsorption
    4. Alcoholism
(Ref. 1, p. 658)
  1. Sodium is:
    1. The principal cation in extracellular fluid
    2. Involved in regulation of plasma volume
    3. Regulated by aldosterone
    4. All of the above
(Ref. 1, p. 658)
81 A
82 B
83 D
84 C
85 D
86 D
87 B
88 A
244
  1. All the following affect nerve and muscle function except:
    1. Calcium
    2. Phosphorus
    3. Sodium
    4. Potassium
(Ref. 1, p. 658)
  1. Potassium:
    1. Is present in higher concentration in extracellular fluid than in intracellular fluid
    2. Retention is increased by aldosterone
    3. Deficiency can cause muscular weakness and paralysis
    4. Is obtained mainly from table salt (Ref. 1, p. 658)
  1. Potassium deficiency can occur:
    1. Following diuretic therapy
    2. In recurrent vomiting
    3. In chronic diarrhoea
    4. In alcoholism
(Ref. 1, p. 658)
  1. Iodine is present in all of the following except:
    1. Thyroglobulin
    2. Thyroxine
    3. Thyroperoxidase
    4. Tri-iodothyronine
(Ref. 1, p. 659)
  1. Copper:
    1. Deficiency can occur in Menkes' disease
    2. Deposition can occur in Wilson's disease
    3. Is transported in circulation by albumin
    4. All of the above are correct
(Ref. 1, p. 659)
  1. Zinc deficiency can lead to:
    1. Hypogonadism
    2. Growth failure
    3. Impaired taste acuity
    4. All of the above
(Ref. 1, p.659)
  1. Acrodermatitis enteropathica can lead to deficiency of:
    1. Zinc
    2. Copper
    3. Selenium
    4. All of the above
(Ref. 1, p. 659)
90 B
91 C
92 A
93 C
94 D
95 D
96 A
245
  1. Impaired glucose tolerance can occur in deficiency of:
    1. Zinc
    2. Chromium
    3. Copper
    4. None of the above
(Ref. 1, p. 659)
  1. Glucose tolerance factor contains:
    1. Selemium
    2. Chromium
    3. Zinc
    4. Copper
(Ref. 1, p. 659)
  1. All the following statements about fluoride are true except:
    1. It is essential for human beings
    2. It increases the hardness of bones
    3. It prevents dental caries
    4. Its excess can cause dental fluorosis
(Ref. 1, p. 659)
  1. Menkes' disease and Wilson's disease have all the following similarities except:
    1. The defective enzyme is copper-binding P-type ATPase in both
    2. Liver copper is increased in both
    3. Serum copper is decreased in both
    4. Serum ceruloplasmin is decreased in both
(Ref. 1, p. 744)
97 B
98 B
99 A
100 B

Water and Electrolyte Balance20

  1. In adults, water constitutes about:
    1. 50% of body weight
    2. 55% of body weight
    3. 60% of body weight
    4. 75% of body weight
(Ref. 6, p. 388)
  1. Of the total body water, intracellular compartment contains about:
    1. 50%
    2. 60%
    3. 70%
    4. 80%
(Ref. 6, p. 388)
  1. Osmotically active substances in plasma are:
    1. Sodium
    2. Chloride
    3. Proteins
    4. All of the above
(Ref. 6, p. 389)
  1. Osmotic pressure of plasma is:
    1. 80-100 milliosmole/litre
    2. 180-200 milliosmole/litre
    3. 280-300 milliosmole/litre
    4. 380-400 milliosmole/litre
(Ref. 6, pp. 29, 389)
  1. Contribution of albumin to colloid osmotic pressure of plasma is about:
    1. 10%
    2. 50%
    3. 80%
    4. 90%
(Ref. 6, p. 29)
1 C
2 C
3 D
4 C
5 C
247
  1. The highest concentration of proteins is present in:
    1. Plasma
    2. Interstitial fluid
    3. Intracellular fluid
    4. Transcellular fluid
(Ref. 6, p. 389)
  1. Oncotic pressure of plasma is due to:
    1. Proteins
    2. Chloride
    3. Sodium
    4. All of the above
(Ref. 6, pp. 29, 389)
  1. Oncotic pressure of plasma is about:
    1. 10 mm of Hg
    2. 15 mm of Hg
    3. 25 mm of Hg
    4. 50 mm of Hg
(Ref. 6, pp. 29, 389)
  1. Oedema can occur when:
    1. Plasma Na and Cl are decreased
    2. Plasma Na and Cl are increased
    3. Plasma proteins are decreased
    4. Plasma proteins are increased
(Ref. 6, p. 29)
  1. Colloid osmotic pressure of intracellular fluid is:
    1. Equal to that of plasma
    2. More than that of plasma
    3. Less than that of plasma
    4. Nearly zero
(Ref. 6, p. 389)
  1. The water produced during metabolic reactions in an adult is about:
    1. 100 ml/day
    2. 300 ml/day
    3. 500 ml/day
    4. 700 ml/day
(Ref. 6, p. 388)
  1. The daily water loss through gastrointestinal tract in an adult is about:
    1. Less than 100 ml/day
    2. 200 ml/day
    3. 300 ml/day
    4. 400 ml/day
(Ref. 6, p. 388)
6 C
7 A
8 C
9 C
10 B
11 B
12 A
248
  1. Recurrent vomiting leads to loss of:
    1. Potassium
    2. Chloride
    3. Bicarbonate
    4. All of the above
(Ref. 6, p. 386)
  1. Obligatory reabsorption of water:
    1. Is about 50% of the total tubular reabsorption of water
    2. Is increased by antidiuretic hormone
    3. Occurs in distal convoluted tubules
    4. Is secondary to reabsorption of solutes
(Ref. 6, p. 528)
  1. Antidiuretic hormone:
    1. Is secreted by hypothalamus
    2. Secretion is increased when osmolality of plasma decreases
    3. Increases obligatory reabsorption of water
    4. Acts on distal convoluted tubules and collecting ducts
(Ref. 6, p. 528)
  1. Urinary water loss is increased in:
    1. Diabetes mellitus
    2. Diabetes insipidus
    3. Chronic glomerulonephritis
    4. All of the above
(Ref. 6, p. 529)
  1. Diabetes insipidus results from:
    1. Decreased insulin secretion
    2. Decreased ADH secretion
    3. Decreased aldosterone secretion
    4. Unresponsiveness of osmoreceptors
(Ref. 1, p. 559)
  1. Thiazide diuretics inhibit:
    1. Carbonic anhydrase
    2. Aldosterone secretion
    3. ADH secretion
    4. Sodium reabsorption in distal tubules
(Ref. 6, p. 528)
13 B
14 D
15 D
16 D
17 B
18 D
249
  1. Furosemide inhibits reabsorption of sodium and chloride in:
    1. Proximal convoluted tubules
    2. Loop of Henle
    3. Distal convoluted tubules
    4. Collecting ducts
(Ref. 6, p. 528)
  1. A diuretic which is an aldosterone antagonist is:
    1. Spironolactone
    2. Ethacrynic acid
    3. Acetazolamide
    4. Chlorothiazide
(Ref. 6, p. 528)
  1. Maximum amount of water per gm of a nutrient is formed from oxidation of:
    1. Carbohydrate
    2. Protein
    3. Fat
    4. Equal from all
(Ref. 6. p. 388)
  1. Osmolality of plasma is expressed in terms of:
    1. Milliosmoles / gm
    2. Milliosmoles / ml
    3. Milliosmoles / kg
    4. Milliosmoles / litre
(Ref. 6, p. 390)
  1. Contribution of proteins to osmolality of plasma is about:
    1. 1%
    2. 10%
    3. 50%
    4. 80%
(Ref. 6, p. 390)
  1. If an impermeable solute like mannitol is introduced into circulation:
    1. Plasma sodium will increase
    2. Plasma sodium will decrease
    3. Blood volume will decrease
    4. None of the above
(Ref. 6, p. 390)
  1. Water and electrolyte balance is regulated by:
    1. Aldosterone
    2. Anti-diuretic hormone
    3. Renin-angiotensin system
    4. All of the above
(Ref. 6, p. 390)
19 B
20 A
21 C
22 C
23 A
24 B
25 D
250
  1. Atrial natriuretic peptides:
    1. Increase urinary sodium excretion
    2. Decrease renin secretion
    3. Decrease aldosterone secretion
    4. All of the above
(Ref. 6, p. 391)
  1. In hypotonic contraction of extracellular fluid:
    1. Plasma sodium is decreased
    2. Osmolality of blood is decreased
    3. Decrease in sodium is more than that in water
    4. All of the above
(Ref. 6, p. 391)
  1. In isotonic contraction of extracellular fluid:
    1. Water shifts from extracellular to intracellular compartment
    2. Water shifts from intracellular to extracellular compartment
    3. Fluid isotonic with plasma is lost
    4. Urine output is increased (Ref. 6, p. 392)
  1. Hypotonic contraction of extracellular fluid can result from:
    1. Vomiting
    2. Diarrhoea
    3. Addison's disease
    4. All of the above
(Ref. 6, p.392)
  1. Diabetes insipidus can cause:
    1. Hypertonic contraction of extracellular fluid
    2. Isotonic contraction of extracellular fluid
    3. Hypotonic contraction of extracellular fluid
    4. Any of the above depending upon severity of the disease
(Ref. 6, p. 392)
26 D
27 D
28 C
29 C
30 A

Acid-base Balance21

  1. In a solution having a pH of 7.4, the hydrogen ion concentration is:
    1. 7.4 nmol/L
    2. 40 nmol/L
    3. 56 nmol/L
    4. 80 nmol/L
(Ref. 6, p. 379)
  1. At pH 7.4, the ratio of bicarbonate: dissolved CO2 is:
    1. 1:1
    2. 10:1
    3. 20:1
    4. 40:1
(Ref. 6, p. 380)
  1. Quantitatively, the most significant buffer system in plasma is:
    1. Phosphate buffer system
    2. Carbonic acid-bicarbonate buffer system
    3. Lactic acid-lactate buffer system
    4. Protein buffer system
(Ref. 6, p. 380)
  1. In a solution containing phosphate buffer, the pH will be 7.4 if the ratio of monohydrogen phosphate: dihydrogen phosphate is:
    1. 4:1
    2. 5:1
    3. 10:1
    4. 20:1
(Ref. 6, p. 381)
  1. pKa of dihydrogen phosphate is:
    1. 5.8
    2. 6.1
    3. 6.8
    4. 7.1
(Ref. 6, p. 381)
1 B
2 C
3 B
4 A
5 C
252
  1. Buffering action of haemoglobin is mainly due to its:
    1. Glutamine residues
    2. Arginine residues
    3. Histidine residues
    4. Lysine residues
(Ref. 5, p. 922)
  1. Respiratory acidosis results from:
    1. Retention of carbon dioxide
    2. Excessive elimination of carbon dioxide
    3. Retention of bicarbonate
    4. Excessive elimination of bicarbonate
(Ref. 5, p. 930)
  1. Respiratory acidosis can occur in all of the following except:
    1. Pulmonary oedema
    2. Hysterical hyperventilation
    3. Pneumothorax
    4. Emphysema
(Ref. 5, p. 931)
  1. The initial event in respiratory acidosis is:
    1. Decrease in pH
    2. Increase in pCO2
    3. Increase in plasma bicarbonate
    4. Decrease in plasma bicarbonate
(Ref. 5, p. 930)
  1. Respiratory alkalosis can occur in:
    1. Bronchial asthma
    2. Collapse of lungs
    3. Hysterical hyperventilation
    4. Bronchial obstruction
(Ref. 6, p. 386)
  1. The primary event in respiratory alkalosis is:
    1. Rise in pH
    2. Decrease in pCO2
    3. Increase in plasma bicarbonate
    4. Decrease in plasma chloride
(Ref. 5, p. 934)
6 C
7 A
8 B
9 B
10 C
11 B
253
  1. Anion gap is the difference in the plasma concentrations of:
    1. (Chloride)–(Bicarbonate)
    2. (Sodium)–(Chloride)
    3. (Sodium+Potassium)–(Chloride+Bicarbonate)
    4. (Sum of cations)–(Sum of anions) (Ref. 6, p. 385)
  1. Normal anion gap in plasma is about:
    1. 5 mEq/L
    2. 15 mEq/L
    3. 25 mEq/L
    4. 40 mEq/L
(Ref. 6 p. 385)
  1. Anion gap is normal in:
    1. Hyperchloraemic metabolic acidosis
    2. Diabetic ketoacidosis
    3. Lactic acidosis
    4. Uraemic acidosis
(Ref. 6, p. 385)
  1. Anion gap is increased in:
    1. Renal tubular acidosis
    2. Metabolic acidosis resulting from diarrhoea
    3. Metabolic acidosis resulting from intestinal obstruction
    4. Diabetic ketoacidosis (Ref. 6, p. 385)
  1. Anion gap in plasma is because:
    1. Of differential distribution of ions across cell membranes
    2. Cations outnumber anions in plasma
    3. Anions outnumber cations in plasma
    4. Of unmeasured anions in plasma
(Ref. 6, pp. 384-385)
  1. Salicylate poisoning can cause:
    1. Respiratory acidosis
    2. Metabolic acidosis with normal anion gap
    3. Metabolic acidosis with increased anion gap
    4. Metabolic alkalosis (Ref. 5, p. 928)
12 C
13 B
14 A
15 D
16 D
17 C
254
  1. Anion gap of plasma can be due to the presence of all of the following except:
    1. Bicarbonate
    2. Lactate
    3. Pyruvate
    4. Citrate
(Ref. 6, pp. 384-385)
  1. All the following features are found in blood chemistry in uncompensated lactic acidosis except:
    1. pH is decreased
    2. Bicarbonate is decreased
    3. pCO2 is normal
    4. Anion gap is normal
(Ref. 6, pp. 384-385)
  1. All the following statements about renal tubular acidosis are correct except:
    1. Renal tubules may be unable to reabsorb bicarbonate
    2. Renal tubules may be unable to secrete hydrogen ions
    3. Plasma chloride is elevated
    4. Anion gap is decreased (Ref. 6, p. 385)
  1. All the following changes in blood chemistry can occur in severe diarrhoea except:
    1. Decreased pH
    2. Decreased bicarbonate
    3. Increased pCO2
    4. Increased chloride
(Ref. 6, pp. 384-385)
  1. During compensation of respiratory alkalosis, all the following changes occur except:
    1. Decreased secretion of hydrogen ions by renal tubules
    2. Increased excretion of sodium in urine
    3. Increased excretion of bicarbonate in urine
    4. Increased excretion of ammonia in urine
(Ref. 6, pp. 381-384)
  1. Blood chemistry shows the following changes in compensated respiratory acidosis:
    1. Increased pCO2
    2. Increased bicarbonate
    3. Decreased chloride
    4. All of the above
(Ref. 6, pp. 384-386)
18 A
19 D
20 D
21 C
22 D
23 D
255
  1. Metabolic alkalosis can occur in:
    1. Severe diarrhoea
    2. Renal failure
    3. Recurrent vomiting
    4. Excessive use of carbonic anhydrase inhibitors
(Ref. 6, p. 386)
  1. All the following features are present in blood chemistry in uncompensated metabolic alkalosis except:
    1. Increased pH
    2. Increased bicarbonate
    3. Normal chloride
    4. Normal pCO2
(Ref. 6, pp. 384, 386)
  1. pH of body fluids is maintained by:
    1. Chemical buffers
    2. Respiratory system
    3. Kidneys
    4. All of the above
(Ref. 6, p. 378)
  1. pKa :
    1. Depends upon dissociation constant of the acid
    2. Is the pH at which the acid is half ionised
    3. Of weak acids is high
    4. All of the above are correct (Ref. 6, p. 378)
  1. The normal hydrogen ion concentration in plasma is:
    1. 7.35 – 7.45 nmol/litre
    2. 35 – 45 nmol/litre
    3. 7.35 – 7.45 mmol/litre
    4. 35 – 45 mmol/litre
(Ref. 6, p. 379)
  1. pH of intracellular fluid:
    1. Is lower than that of plasma
    2. Is equal to that of plasma
    3. Is higher than that of plasma
    4. Has no effect on cellular function
(Ref. 6, p. 383)
  1. Metabolic acidosis can occur in all of the following except:
    1. Diabetes mellitus
    2. Vomiting
    3. Diarrhoea
    4. Addison's disease
(Ref. 6, p. 386)
24 C
25 C
26 D
27 D
28 B
29 A
30 B

Nutrition and Diet22

  1. One joule is the energy required to:
    1. Raise the temperature of 1 gm of water by 1 C
    2. Raise the temperature of 1 kg of water by 1 C
    3. Move a mass of 1 gm by 1 cm distance by a force of 1 Newton
    4. Move a mass of 1 kg by 1 metre distance by a force of 1 Newton
(Ref. 4, p. 542)
  1. 1 kcal is roughly equal to:
    1. 4.2 J
    2. 42 J
    3. 4.2 KJ
    4. 42 KJ
(Ref. 4, p. 542)
  1. Calorific value of proteins as determined in a bomb calorimeter is:
    1. 4 kcal/gm
    2. 4.8 kcal/gm
    3. 5.4 kcal/gm
    4. 5.8 kcal/gm
(Ref. 1, p. 654)
  1. Calorific value of proteins in a living person is less than that in a bomb calorimeter because:
    1. Digestion and absorption of proteins is less than 100%
    2. Respiratory quotient of proteins is less than 1
    3. Specific dynamic action of proteins is high
    4. Proteins are not completely oxidised in living persons
(Ref. 4, p. 542)
  1. Calorific value of alcohol is:
    1. 4 kcal/gm
    2. 5.4 kcal/gm
    3. 7 kcal/gm
    4. 9 kcal/gm
(Ref. 4, p. 542)
1 D
2 C
3 C
4 D
5 C
257
  1. Energy expenditure of a person can be measured by:
    1. Bomb calorimetry
    2. Direct calorimetry
    3. Indirect calorimetry
    4. Direct or indirect calorimetry
(Ref. 4, pp. 542-543)
  1. Respiratory quotient of carbohydrates is about:
    1. 0.5
    2. 0.7
    3. 0.8
    4. 1.0
(Ref. 4, p. 543)
  1. Respiratory quotient of fats is about:
    1. 0.5
    2. 0.7
    3. 0.8
    4. 1.0
(Ref. 4, p. 543)
  1. Respiratory quotient of proteins is about:
    1. 0.5
    2. 0.7
    3. 0.8
    4. 1.0
(Ref. 4, p. 543)
  1. Respiratory quotient of an average mixed diet is about:
    1. 0.65
    2. 0.7
    3. 0.75
    4. 0.85
(Ref. 4, p. 543)
  1. At a respiratory quotient of 0.85, every litre of oxygen consumed represents an energy expenditure of:
    1. 5.825 kcal
    2. 4.825 kcal
    3. 3.825 kcal
    4. 2.825 kcal
(Ref. 4, p. 545)
  1. BMR of healthy adult men is about:
    1. 30 kcal/hour/square metre
    2. 35 kcal/hour/square metre
    3. 40 kcal/hour/square metre
    4. 45 kcal/hour/square metre
(Ref. 5, p. 853)
  1. BMR of healthy adult women is about:
    1. 32 kcal/hour/square metre
    2. 36 kcal/hour/square metre
    3. 40 kcal/hour/square metre
    4. 44 kcal/hour/square metre
(Ref. 5, p. 853)
6 D
7 D
8 B
9 C
10 D
11 B
12 C
13 B
258
  1. BMR is higher in:
    1. Adults than in children
    2. Men than in women
    3. Vegetarians than in non-vegetarians
    4. Warmer climate than in colder climate
(Ref. 4, p. 544)
  1. BMR is decreased in:
    1. Pregnancy
    2. Starvation
    3. Anaemia
    4. Fever
(Ref. 4, p. 544)
  1. BMR is increased in:
    1. Starvation
    2. Hypothyroidism
    3. Addison's disease
    4. Pregnancy
(Ref. 5, p. 855)
  1. BMR is decreased in all of the following except:
    1. Fever
    2. Addison's disease
    3. Starvation
    4. Hypothyroidism
(Ref. 4, pp. 544-545)
  1. BMR is increased in all of the following except:
    1. Hyperthyroidism
    2. Anaemia
    3. Addison's disease
    4. Pregnancy
(Ref. 5, pp. 854-855)
  1. Specific dynamic action of carbohydrates is about:
    1. 5%
    2. 13%
    3. 20%
    4. 30%
(Ref. 4, p. 546)
  1. Specific dynamic action of proteins is about:
    1. 5%
    2. 13%
    3. 20%
    4. 30%
(Ref. 4, p. 546)
  1. Specific dynamic action of a mixed diet is about:
    1. 5%
    2. 10%
    3. 15%
    4. 20%
(Ref. 4, p. 546)
  1. After accounting for SDA, the net gain of energy from 25 gm of proteins is about:
    1. 70 kcal
    2. 100 kcal
    3. 130 kcal
    4. 200 kcal
(Ref. 4, p. 546)
14 B
15 B
16 D
17 A
18 C
19 A
20 D
21 B
22 A
259
  1. After accounting for SDA, the net gain of energy from 25 gm of carbohydrates is about:
    1. 70 kcal
    2. 95 kcal
    3. 100 kcal
    4. 105 kcal
(Ref. 4, p. 546)
  1. After accounting for SDA, the net gain of energy from 100 gm of fats is about:
    1. 600 kcal
    2. 780 kcal
    3. 900 kcal
    4. 1020 kcal
(Ref. 4, p. 546)
  1. If proteins, carbohydrates and fats are consumed together:
    1. The total SDA is the sum of individual SDAs of proteins, carbohydrates and fats
    2. The total SDA is more than the sum of individual SDAs of proteins, carbohydrates and fats
    3. Carbohydrates and fats lower the SDA of proteins
    4. Proteins raise the SDA of carbohydrates and fats
(Ref. 4, p. 546)
  1. After calculating the energy requirement of a person:
    1. 10% kcal are subtracted on account of SDA
    2. 10% kcal are added on account of SDA
    3. 20% kcal are subtracted on account of SDA
    4. 20% kcal are added on account of SDA
(Ref. 4, p. 546)
  1. The largest variable affecting energy expenditure of an individual is:
    1. Environmental temperature
    2. Physical activity
    3. Basal metabolic requirement
    4. Specific dynamic action of food
(Ref. 1, p.655)
  1. Cysteine can partially spare the requirement for:
    1. Methionine
    2. Phenylalanine
    3. Tyrosine
    4. None of the above
(Ref. 1, p.654)
23 B
24 B
25 C
26 B
27 B
28 A
260
  1. During pregnancy, the following should be added to the calculated energy requirement:
    1. 300 kcal/day
    2. 500 kcal/day
    3. 700 kcal/day
    4. 900 kcal/day
(Ref. 6, p. 446)
  1. During lactation, the following should be added to the calculated energy requirement:
    1. 100 kcal / day
    2. 300 kcal / day
    3. 500 kcal / day
    4. 700 kcal / day
(Ref. 6, p.446)
  1. Energy - yielding nutrients are:
    1. Vitamins and minerals
    2. Proteins
    3. Carbohydrates and fats
    4. Carbohydrates, fats and proteins
(Ref. 1, p.653)
  1. The limiting amino acid in wheat is:
    1. Leucine
    2. Lysine
    3. Cysteine
    4. Methionine
(Ref. 5, p. 867)
  1. The limiting amino acid in pulses is:
    1. Leucine
    2. Lysine
    3. Tryptophan
    4. Methionine
(Ref. 6, p. 451)
  1. Maize is poor in:
    1. Lysine
    2. Methionine
    3. Tryptophan
    4. Lysine and tryptophan
(Ref. 1, p. 656)
  1. The percentage of ingested protein/nitrogen absorbed into blood stream is known as:
    1. Net protein utilisation
    2. Protein efficiency ratio
    3. Digestibility coefficient
    4. Biological value of protein
(Ref. 5, p. 654)
29 A
30 C
31 D
32 B
33 D
34 D
35 C
261
  1. Biological value of a protein is:
    1. The percentage of ingested protein/nitrogen absorbed into circulation
    2. The percentage of ingested protein/nitrogen retained in the body
    3. The percentage of ingested protein utilised for protein synthesis in the body
    4. The gain in body weight (gm) per gm of protein ingested
(Ref. 5, p. 863)
  1. Net protein utilisation depends upon:
    1. Protein efficiency ratio
    2. Digestibility coefficient
    3. Digestibility coefficient and protein efficiency ratio
    4. Digestibility coefficient and biological value
(Ref. 5, p. 864)
  1. The gain in body weight (gm) per gm of protein ingested is known as:
    1. Net protein utilisation
    2. Protein efficiency ratio
    3. Digestibility coefficient
    4. Biological value of protein
(Ref. 5, p. 863)
  1. The following is considered as reference standard for comparing the nutritional quality of proteins:
    1. Milk proteins
    2. Egg proteins
    3. Meat proteins
    4. Fish proteins
(Ref. 5, p. 865)
  1. Biological value of egg proteins is about:
    1. 70%
    2. 80%
    3. 86%
    4. 94%
(Ref. 5, p. 864)
  1. The following has the highest protein efficiency ratio:
    1. Milk proteins
    2. Egg proteins
    3. Meat proteins
    4. Fish proteins
(Ref. 6, p. 451)
  1. The following has the lowest protein efficiency ratio:
    1. Maize proteins
    2. Wheat proteins
    3. Milk proteins
    4. Rice proteins
(Ref. 6, p. 451)
36 B
37 D
38 B
39 B
40 D
41 B
42 A
262
  1. Protein content of egg is about:
    1. 10%
    2. 13%
    3. 16%
    4. 20%
(Ref. 6, p. 455)
  1. Protein content of meat is about:
    1. 10%
    2. 13%
    3. 16%
    4. 20%
(Ref. 6, p. 455)
  1. Protein content of rice is about:
    1. 7%
    2. 12%
    3. 15%
    4. 20%
(Ref. 6, p. 567)
  1. Highest protein content amongst the following is present in:
    1. Wheat
    2. Rice
    3. Pulses
    4. Soyabean
(Ref. 6, p. 567)
  1. Daily protein requirement of an adult man is:
    1. 0.5 gm/kg of body weight
    2. 0.8 gm/kg of body weight
    3. 1.0 gm/kg of body weight
    4. 1.5 gm/kg of body weight
(Ref. 5, p. 869)
  1. Daily protein requirement of an adult woman is:
    1. 0.5 gm/kg of body weight
    2. 0.8 gm/kg of body weight
    3. 1.0 gm/kg of body weight
    4. 1.5 gm/kg of body weight
(Ref. 5, p. 869)
  1. Exposure to sunlight decreases the requirement of:
    1. Vitamin A
    2. Vitamin E
    3. Vitamin D
    4. Vitamin K
(Ref. 1, p. 654)
  1. Invisible fat is present in:
    1. Milk
    2. Coconut oil
    3. Groundnut oil
    4. Hydrogenated oils
(Ref. 6, p. 656)
  1. Visible fat is present in:
    1. Milk
    2. Pulses
    3. Coconut oil
    4. Egg yolk
(Ref. 6, p. 448)
43 B
44 D
45 A
46 D
47 C
48 C
49 C
50 A
51 C
263
  1. Fat content of eggs is about:
    1. 7%
    2. 10%
    3. 13%
    4. 16%
(Ref. 6, p. 454)
  1. Fat content of pulses is about:
    1. 5%
    2. 10%
    3. 15%
    4. 20%
(Ref. 6, p. 454)
  1. Predominant fatty acids in meat are:
    1. Saturated
    2. Monounsaturated
    3. Polyunsaturated
    4. Mono- and poly-unsaturated
(Ref. 2, p. 759)
  1. Amongst the following, the highest PUFA content is present in:
    1. Safflower oil
    2. Cottonseed oil
    3. Groundnut oil
    4. Coconut oil
(Ref. 6, p.448)
  1. Cholesterol is present in all of the following except:
    1. Egg
    2. Fish
    3. Milk
    4. Pulses
(Ref. 1, p. 657)
  1. Amongst the following the highest cholesterol content is found in:
    1. Meat
    2. Fish
    3. Butter
    4. Milk
(Ref. 6, p. 449)
  1. The following has the highest cholesterol content:
    1. Egg yolk
    2. Egg white
    3. Meat
    4. Fish
(Ref. 6, p. 449)
  1. Amongst the following, the least cholesterol content is found in:
    1. Milk
    2. Meat
    3. Butter
    4. Cheese
(Ref. 6, p. 656)
  1. The following constitutes fibre or roughage in food:
    1. Cellulose
    2. Pectin
    3. Inulin
    4. All of the above
(Ref. 1, p. 656)
  1. The starch content of wheat is about:
    1. 50%
    2. 60%
    3. 70%
    4. 80%
(Ref. 5, p. 888)
52 C
53 A
54 A
55 A
56 D
57 C
58 A
59 A
60 D
61 C
264
  1. The starch content of pulses is about:
    1. 50%
    2. 60%
    3. 70%
    4. 80%
(Ref. 6, p. 454)
  1. A significant source of starch among vegetables is:
    1. Radish
    2. Spinach
    3. Potato
    4. Cauliflower
(Ref. 6, p. 454)
  1. The calorific value of wheat is about:
    1. 2.5 kcal/gm
    2. 3.5 kcal/gm
    3. 4.5 kcal/gm
    4. 5.5 kcal/gm
(Ref. 5, p. 888)
  1. For vegetarians, pulses are an important source of:
    1. Carbohydrates
    2. Proteins
    3. Fat
    4. Iron
(Ref. 5, p. 887)
  1. The amino acids present in pulses can supplement the limiting amino acids of:
    1. Cereals
    2. Milk
    3. Fish
    4. Nuts and beans
(Ref. 6, p. 451)
  1. Milk is a good source of:
    1. Proteins, calcium and iron
    2. Proteins, calcium and ascorbic acid
    3. Proteins, lactose and retinol
    4. Proteins, lactose and essential fatty acids
(Ref. 5, pp. 883-884)
  1. Milk is a good source of all of the following except:
    1. Essential amino acids
    2. Vitamin C
    3. Galactose
    4. Calcium and phosphorus
(Ref. 5, p. 884)
  1. Milk is poor in:
    1. Cholesterol
    2. Retinol
    3. Calcium
    4. Iron
(Ref. 5, p. 884)
62 B
63 C
64 B
65 B
66 A
67 C
68 B
69 D
265
  1. Egg is rich in all of the following except:
    1. Cholesterol
    2. Saturated fatty acids
    3. Ascorbic acid
    4. Calcium
(Ref. 5, p. 887)
  1. A phosphoprotein present in egg is:
    1. Casein
    2. Albumin
    3. Ovoglobulin
    4. Ovovitellin
(Ref. 5, p. 886)
  1. Consumption of raw eggs can cause deficiency of:
    1. Calcium
    2. Lipoic acid
    3. Biotin
    4. Vitamin A
(Ref. 1, p. 635)
  1. Egg is poor in:
    1. Essential amino acids
    2. Carbohydrates
    3. Avidin
    4. Biotin
(Ref. 6, p. 454)
  1. Cholesterol is present in all of the following except:
    1. Milk
    2. Fish
    3. Egg white
    4. Egg yolk
(Ref. 5, p. 886)
  1. Meat is rich in all of the following except:
    1. Iron
    2. Fluorine
    3. Copper
    4. Zinc
(Ref. 6, pp. 435, 438, 440-442)
  1. Kwashiorkor occurs when the diet is severely deficient in:
    1. Iron
    2. Calories
    3. Proteins
    4. Essential fatty acids
(Ref. 1, p. 656)
  1. Clinical features of kwashiorkor include all of the following except:
    1. Mental retardation
    2. Muscle wasting
    3. Oedema
    4. Anaemia
(Ref. 5, pp. 879-880)
  1. Kwashiorkor usually occurs in:
    1. The post-weaning period
    2. Pregnancy
    3. Lactation
    4. Old age
(Ref. 5, p. 879)
70 C
71 D
72 C
73 B
74 C
75 B
76 C
77 A
78 A
266
  1. Marasmus occurs from deficient intake of:
    1. Essential amino acids
    2. Essential fatty acids
    3. Calories
    4. Zinc
(Ref. 5, p. 879)
  1. Marasmus differs from kwashiorkor in the following respect:
    1. Mental retardation occurs in kwashiorkor but not in marasmus
    2. Growth in retarded in kwashiorkor but not in marasmus
    3. Muscle wasting occurs in marasmus but not in kwashiorkor
    4. Subcutaneous fat disappears in marasmus but not in kwashiorkor
(Ref. 5, pp. 879-880)
  1. Energy reserves of an average well-fed adult man are about:
    1. 50,000 kcal
    2. 100,000 kcal
    3. 200,000 kcal
    4. 300,000 kcal
(Ref. 6, p. 245)
  1. During starvation, the first reserve nutrient to be depleted is:
    1. Glycogen
    2. Proteins
    3. Triglycerides
    4. Cholesterol
(Ref. 2, p. 776)
  1. All of the following are decreased in starvation except:
    1. Blood glucose
    2. Plasma free fatty acids
    3. Basal metabolic rate
    4. Liver glycogen
(Ref. 1, pp. 302, 655)
  1. During starvation, ketone bodies are used as a fuel by:
    1. Erythrocytes
    2. Brain
    3. Liver
    4. All of the above
(Ref. 2, pp. 776-777)
79 C
80 D
81 B
82 A
83 B
84 B
267
  1. Animal fat is in general:
    1. Poor in saturated and rich in polyunsaturated fatty acids
    2. Rich in saturated and poor in polyunsaturated fatty acids
    3. Rich in saturated and polyunsaturated fatty acids
    4. Poor in saturated and polyunsaturated fatty acids
(Ref. 3, p. 759)
  1. In the diet of a diabetic patient, the recommended carbohydrate intake should preferably be in the form of:
    1. Monosaccharides
    2. Disaccharides
    3. Polysaccharides
    4. Any of the above
(Ref. 6, p. 456)
  1. Obesity increases the risk of:
    1. Hypertension
    2. Diabetes mellitus
    3. Cardiovascular disease
    4. All of the above
(Ref. 3, p. 762)
  1. Worldwide, the most common vitamin deficiency is that of:
    1. Ascorbic acid
    2. Folic acid
    3. Vitamin A
    4. Vitamin D
(Ref. 3, p. 772)
  1. Consumption of iodised salt is recommended for prevention of:
    1. Hypertension
    2. Hyperthyroidism
    3. Endemic goitre
    4. None of the above
(Ref. 3, p. 782)
  1. Restriction of salt intake is generally recommended in:
    1. Diabetes mellitus
    2. Hypertension
    3. Cirrhosis of liver
    4. Peptic ulcer
(Ref. 6, p. 456)
  1. The correct increasing order of calorific values is:
    1. Carbohydrate, ethanol and fat
    2. Carbohydrate, fat and ethanol
    3. Fat, ethanol and carbohydrate
    4. Ethanol, fat and carbohydrate
(Ref. 1, p. 654)
85 B
86 C
87 D
88 B
89 C
90 B
91 A
268
  1. The following has the highest calorific value:
    1. Carbohydrate
    2. Protein
    3. Fat
    4. Ethanol
(Ref. 1, p. 654)
  1. Energy expenditure of an individual is influenced by:
    1. Basal metabolic rate
    2. Specific dynamic action of food
    3. Physical activity
    4. All of the above
(Ref. 1, p. 655)
  1. Amino acids are required to synthesise all of the following except:
    1. Purines
    2. Pyrimidines
    3. Pyridoxine
    4. Haem
(Ref. 1, p. 655)
  1. If sufficient tyrosine is present in diet, it spares the requirement of:
    1. Phenylalanine
    2. Tryptophan
    3. Lysine
    4. None of the above
(Ref. 1, p. 655)
  1. If sufficient linoleic acid is present in diet, it spares the requirement of:
    1. Arachidonic acid
    2. α-Linolenic acid
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 654)
  1. An essential function of dietary lipids is to provide:
    1. Energy
    2. Essential fatty acids
    3. Cholesterol
    4. All of the above
(Ref. 1, p. 657)
  1. Lipids are essential in diet because they:
    1. Act as vehicles for fat-soluble vitamins
    2. Provide essential fatty acids
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 657)
92 C
93 D
94 C
95 A
96 A
97 B
98 C
269
  1. An adequate intake of carbohydrate prevents:
    1. Diabetes mellitus
    2. Ketosis
    3. Kwashiorkor
    4. None of the above
(Ref. 1, p. 656)
  1. A carbohydrate which is essential in diet is:
    1. Glucose
    2. Starch
    3. Galactose
    4. None of the above
(Ref. 1, p. 656)
99 B
100 D

Hormones23

  1. Hormone receptors possess all the following properties except:
    1. All of them are proteins
    2. They possess a recognition domain
    3. They bind hormones with a high degree of specificity
    4. Number of receptors in a target cell is constant
(Ref. 1, pp. 534, 619)
  1. The only correct statement about hormone receptors is:
    1. Receptors for protein hormones are present in cytosol
    2. Receptors for steroid hormones are membrane-bound
    3. Hormone-receptor binding is irreversible
    4. Receptors can undergo downregulation and upregulation
(Ref. 1, pp. 535, 619)
  1. Downregulation is:
    1. Increased destruction of a hormone
    2. Feedback inhibition of hormone secretion
    3. Decreased concentration of a hormone in blood
    4. Decrease in number of receptors for a hormone
(Ref. 1, p. 619)
  1. All the following statements about hormones are true except:
    1. All of them require specific carriers in plasma
    2. All of them require specific receptors in target cells
    3. Some of them are subject to feedback regulation
    4. Some of them increase the transcription of certain genes
(Ref. 1, pp. 534-536, 550)
1 D
2 D
3 D
4 A
271
  1. All the following statements about steroid hormones are true except:
    1. They are hydrophobic
    2. They require carriers to transport them in circulation
    3. Their receptors are intracellular
    4. They require cyclic AMP as second messenger
(Ref. 1, pp. 535-536)
  1. Cyclic AMP acts as the second messenger for:
    1. ADH
    2. Glucagon
    3. Calcitonin
    4. All of the above
(Ref. 1, p. 535)
  1. Cyclic AMP acts as the second messenger for all of the following except:
    1. Oxytocin
    2. TSH
    3. ACTH
    4. FSH
(Ref. 1, p. 535)
  1. Cyclic GMP acts as the second messenger for:
    1. Nerve growth factor
    2. Atrial natriuretic factor
    3. Epinephrine
    4. Norepinephrine
(Ref. 1, p. 535)
  1. Some hormones produce their intracellular effects by activating:
    1. Phospholipase A1
    2. Phospholipase B
    3. Phospholipase C
    4. All of the above
(Ref. 1, p. 546)
  1. Inositol triphosphate is the second messenger for:
    1. Gastrin
    2. Cholecystokinin
    3. Oxytocin
    4. All of the above
(Ref. 1, p. 535)
  1. G-proteins act as:
    1. Hormone carriers
    2. Hormone receptors
    3. Second messengers
    4. Signal transducers
(Ref. 1, pp. 541-543)
  1. Signal transducer for glucagon is a:
    1. Cyclic nucleotide
    2. Phosphoinositide
    3. Stimulatory G-protein
    4. Inhibitory G-protein
(Ref. 1, p. 543)
5 D
6 D
7 A
8 B
9 C
10 D
11 D
12 C
272
  1. G-proteins are:
    1. Monomers
    2. Dimers
    3. Trimers
    4. Tetramers
(Ref. 1, p. 542)
  1. G-proteins have a nucleotide binding site for:
    1. ADP/ATP
    2. GDP/GTP
    3. CDP/CTP
    4. UDP/UTP
(Ref. 1, p. 542)
  1. The nucleotide binding site of G-proteins is present on their:
    1. α-Subunit
    2. β-Subunit
    3. γ-Subunit
    4. δ-Subunit
(Ref. 1, p. 542)
  1. Adenylate cyclase is activated by:
    1. GDP-bearing α-subunit of G-protein
    2. GTP-bearing α-subunit of G-protein
    3. GDP-bearing γ-subunit of G-protein
    4. GTP-bearing γ-subunit of G-protein
(Ref. 2, p. 342)
  1. Tyrosine kinase activity is present in:
    1. A.α-Adrenergic receptors
    2. B.β-Adrenergic receptors
    3. Cholinergic receptors
    4. Insulin receptors
(Ref. 1, pp. 547-548)
  1. Insulin receptor is a:
    1. Monomer
    2. Dimer
    3. Trimer
    4. Tetramer
(Ref. 1, p. 617)
  1. Tyrosine kinase activity is present in:
    1. Acetylcholine receptor
    2. PDGF receptor
    3. ADH receptor
    4. All of the above
(Ref. 1, p. 535)
  1. Protein kinase C is activated by:
    1. Cyclic AMP
    2. Cyclic GMP
    3. Diacyl glycerol
    4. Inositol triphosphate
(Ref. 1, p. 546)
13 C
14 B
15 A
16 B
17 D
18 D
19 B
20 C
273
  1. Melatonin is synthesised in:
    1. Hypothalamus
    2. Posterior pituitary gland
    3. Pineal gland
    4. Melanocytes
(Ref. 1, p. 354)
  1. Melatonin is synthesised from:
    1. Phenylalanine
    2. Tyrosine
    3. Tryptophan
    4. None of the above
(Ref. 1, p. 352)
  1. Melanocyte stimulating hormone is secreted by:
    1. Pineal gland
    2. Anterior lobe of pituitary gland
    3. Posterior lobe of pituitary gland
    4. Intermediate lobe of pituitary gland
(Ref. 5, p. 715)
  1. MSH causes:
    1. Dispersal of melanin granules in melanocytes
    2. Increase in melanin concentration in melanocytes
    3. Decrease in melanin concentration in melanocytes
    4. Increase in number of melanocytes
(Ref. 1, p. 557)
  1. Secretion of MSH is regulated by:
    1. Feedback mechanism
    2. Melatonin
    3. Hypothalamic hormones
    4. ACTH
(Ref. 1, p. 551)
  1. A hormone synthesised in the hypothalamus is:
    1. Melatonin
    2. Melanocyte stimulating hormone
    3. Vasopressin
    4. Prolactin
(Ref. 1, p. 557)
  1. Posterior pituitary gland secretes:
    1. Catecholamines
    2. Oxytocin
    3. Follicle stimulating hormone
    4. Serotonin
(Ref. 1, p. 557)
21 C
22 C
23 D
24 B
25 C
26 C
27 B
274
  1. A nonapeptide among the following is:
    1. Antidiuretic hormone
    2. Insulin
    3. ACTH
    4. Thyrotropin releasing hormone
(Ref. 1, pp. 551, 557, 558, 611)
  1. Diabetes insipidus is caused by deficient secretion of:
    1. Insulin
    2. Glucagon
    3. Vasopressin
    4. Oxytocin
(Ref. 1, p. 559)
  1. Peripheral vasoconstriction is caused by high concentrations of:
    1. Antidiuretic hormone
    2. Melatonin
    3. Glucagon
    4. Oxytocin
(Ref. 1, p. 557)
  1. Somatotropin is secreted by:
    1. Hypothalamus
    2. Anterior pituitary
    3. Posterior pituitary
    4. Thyroid gland
(Ref. 3, p. 726)
  1. Secretion of insulin-like growth factor-I is promoted by:
    1. Insulin
    2. Glucagon
    3. Growth hormone
    4. Somatomedin C
(Ref. 1, p. 553)
  1. Growth hormone increases:
    1. Protein synthesis
    2. Lipogenesis
    3. Glycogenolysis
    4. All of the above
(Ref. 1, p. 553)
  1. Secretion of growth hormone is inhibited by:
    1. Somatomedin C
    2. Somatostatin
    3. Feedback inhibition
    4. All of the above
(Ref. 1, p. 551)
  1. Secretion of somatotropin is promoted by:
    1. Somatomedin C
    2. Somatostatin
    3. Growth hormone releasing hormone
    4. Hypoglycaemia
(Ref. 1, p. 551)
28 A
29 C
30 A
31 B
32 C
33 A
34 B
35 C
275
  1. Human growth hormone has:
    1. One polypeptide chain and one intra-chain disulphide bond
    2. One polypeptide chain and two intra-chain disulphide bonds
    3. Two polypeptide chains joined by one disulphide bond
    4. Two polypeptide chains joined by two disulphide bonds
(Ref. 1, p. 552)
  1. Number of amino acid residues in human growth hormone is:
    1. 51
    2. 84
    3. 191
    4. 198
(Ref. 1, p. 552)
  1. Number of amino acid residues in prolactin is:
    1. 51
    2. 84
    3. 191
    4. 198
(Ref. 1, p. 551)
  1. Secretion of prolactin is regulated by:
    1. Feedback inhibition
    2. Prolactin releasing hormone
    3. Prolactin release inhibiting hormone
    4. All of the above
(Ref. 1, p. 556)
  1. Precursor of ACTH is:
    1. Cholesterol
    2. Pregnenolone
    3. Corticotropin
    4. Pro-opiomelanocortin
(Ref. 1, p. 556)
  1. All of the following can be formed from pro-opiomelano-cortin except:
    1. α- and β-MSH
    2. β- and γ-Lipotropins
    3. α- and β-Endorphins
    4. FSH
(Ref. 1, p. 556)
  1. All the following statements about pro-opiomelanocortin are true except:
    1. It is made up of 285 amino acids
    2. It is synthesised in pars intermedia and anterior lobe of pituitary gland
    3. It is the precursor of ACTH and melatonin
    4. It is the precursor of corticotropin-like intermediate lobe peptide and endorphins
(Ref. 1, pp. 555-556)
36 B
37 C
38 D
39 C
40 D
41 D
42 C
276
  1. All the following statements about ACTH are true except:
    1. It is a tropic hormone
    2. Its target cells are located in adrenal cortex
    3. Its receptors are located in the cell membrane
    4. Its second messenger is inositol triphosphate
(Ref. 1, pp. 556-557)
  1. Regulation of ACTH secretion occurs through:
    1. Corticotropin releasing hormone (CRH) and corticotropin release inhibiting hormone (CRIH) of hypothalamus
    2. Feedback inhibition by cortisol
    3. CRH and feedback inhibition by cortisol
    4. CRIH and feedback inhibition by cortisol
(Ref. 1, pp. 550-551)
  1. ACTH is a polypeptide made up of:
    1. 39 amino acids
    2. 41 amino acids
    3. 51 amino acids
    4. 84 amino acids
(Ref. 1, p. 556)
  1. CRH is a polypeptide made up of:
    1. 39 amino acids
    2. 41 amino acids
    3. 51 amino acids
    4. 84 amino acids
(Ref. 1, p. 551)
  1. Hormonal activity of ACTH is completely lost on removal of:
    1. 5 C-terminal amino acids
    2. 10 C-terminal amino acids
    3. 15 C-terminal amino acids
    4. None of the above
(Ref. 1, p. 556)
  1. All the following statements about TSH are true except:
    1. It is a glycoprotein
    2. It is made up of α-and β-subunits
    3. Receptor recognition involves both the subunits
    4. Its β-subunit is identical with those of FSH and LH
(Ref. 1, p. 555)
43 D
44 C
45 A
46 B
47 D
48 D
277
  1. All the following statements about TSH are true except:
    1. It is a tropic hormone
    2. It acts on para-follicular cells of thyroid gland
    3. Its receptors are membrane-bound
    4. Its second messenger is cyclic AMP
(Ref. 1, pp. 555, 561)
  1. All the following statements about thyrotropin releasing hormone are true except:
    1. It is secreted by hypothalamus
    2. It is a pentapeptide
    3. It increases the secretion of TSH
    4. Its secretion is inhibited by high level of T3 and T4 in blood
(Ref. 1, p. 551)
  1. In males, luteinising hormone acts on:
    1. Leydig cells
    2. Sertoli cells
    3. Prostate gland
    4. All of the above
(Ref. 1, p. 551)
  1. All the following statements about FSH are true except:
    1. It is a tropic hormone secreted by anterior pituitary
    2. Its secretion is increased by gonadotropin releasing hormone
    3. It acts on Sertoli cells
    4. It increases the synthesis of testosterone
(Ref. 1, pp. 551, 555)
  1. In males, secretion of luteinising hormone is inhibited by:
    1. Gonadotropin releasing hormone
    2. FSH
    3. High blood level of testosterone
    4. Inhibin
(Ref. 1, p. 598)
  1. Secretion of luteinising hormone is increased by:
    1. GnRH
    2. FSH
    3. Testosterone
    4. None of the above
(Ref. 1, p. 551)
49 B
50 B
51 A
52 D
53 C
54 A
278
  1. In structure and function, hCG resembles:
    1. FSH
    2. LH
    3. GnRH
    4. Progesterone
(Ref. 1, pp. 555, 604)
  1. Acromegaly results from overproduction of:
    1. ACTH during childhood
    2. TSH during adult life
    3. Growth hormone during childhood
    4. Growth hormone during adult life
(Ref. 1, p. 554)
  1. Acromegaly results in all of the following except:
    1. Overgrowth of the bones of face, hands and feet
    2. Increased stature
    3. Enlargements of viscera
    4. Impaired glucose tolerance
(Ref. 1, p. 554)
  1. Overproduction of growth hormone during childhood causes:
    1. Acromegaly
    2. Gigantism
    3. Cushing's disease
    4. Simmond's disease
(Ref. 1, p. 554)
  1. Decreased secretion of growth hormone during childhood causes:
    1. Simmond's disease
    2. Cushing's disease
    3. Dwarfism
    4. Cretinism
(Ref. 1, p. 554)
  1. Stature is increased in:
    1. Gigantism
    2. Acromegaly
    3. Simmond's disease
    4. Cushing's disease
(Ref. 1, p. 554)
  1. An amino acid used for the synthesis of thyroid hormone is:
    1. Tyrosine
    2. Tryptophan
    3. Histidine
    4. Proline
(Ref. 1, p. 561)
  1. An enzyme required for the synthesis of thyroid hormones is:
    1. Iodinase
    2. Deiodinase
    3. Thyroperoxidase
    4. Thyroxine synthetase
(Ref. 1, pp. 562-563)
55 B
56 D
57 B
58 B
59 C
60 A
61 A
62 C
279
  1. Thyroperoxidase iodinates:
    1. Free tyrosine in thyroid gland
    2. Tyrosine residues of thyroglobulin
    3. Tyrosine residues of thyroxine binding globulin
    4. Tyrosine residues of thyroxine binding prealbumin
(Ref. 1, p. 563)
  1. In thyroxine, tyrosine residues are iodinated at positions:
    1. 1 and 3
    2. 2 and 4
    3. 3 and 5
    4. 4 and 6
(Ref. 1, p. 563)
  1. Thyroid gland takes up circulating iodine:
    1. By simple diffusion
    2. By facilitated diffusion
    3. By active uptake
    4. In exchange for chloride
(Ref. 1, p. 562)
  1. Thyroid hormones are present in blood:
    1. In free from
    2. In association with thyroxine binding globulin (TBG)
    3. In association with thyroxine binding pre-albumin (TBPA)
    4. Mainly in association with TBG, partly in free form and sometimes in association with TBPA also
(Ref. 1, p. 564)
  1. When thyroxine binding globulin and thyroxine binding pre-albumin are saturated with thyroxine, the excess hormone is transported by:
    1. Albumin
    2. Gamma globulins
    3. Transcortin
    4. None of the above
(Ref. 5, p. 724)
  1. Receptors for thyroid hormones are present:
    1. On the cell membrane
    2. Across the cell membrane
    3. Inside the cells
    4. In association with G-proteins
(Ref. 1, pp. 564-565)
63 B
64 C
65 C
66 D
67 A
68 C
280
  1. Binding of thyroxine to its receptors:
    1. Activates adenylate cyclase
    2. Activates guanylate cyclase
    3. Activates a stimulatory G-protein
    4. Increases transcription
(Ref. 1, p. 565)
  1. The most powerful thyroid hormone is:
    1. Reverse T3
    2. DIT
    3. T3
    4. T4
(Ref. 1, p. 564)
  1. The most abundant thyroid hormone in blood is:
    1. Free T3
    2. T3 bound to TBG
    3. Free T4
    4. T4 bound to TBG
(Ref. 1, p. 564)
  1. Secretion of thyroid hormones is regulated by:
    1. Hypothalamus
    2. Anterior pituitary
    3. Feedback regulation
    4. All of the above
(Ref. 1, p. 551)
  1. Clinical features of hyperthyroidism include:
    1. Goitre, heat intolerance, weight loss and tachycardia
    2. Goitre, tremors, tachycardia and cold intolerance
    3. Exophthalmos, goitre, tachycardia and loss of appetite
    4. Exophthalmos, goitre, tremors and obesity
(Ref. 1, p. 565)
  1. All the following may occur in hyperthyroidism except:
    1. Goitre
    2. Increased appetite
    3. Loss of weight
    4. Low BMR
(Ref. 1, p. 565)
  1. All the following may occur in myxoedema except:
    1. Cold intolerance
    2. Low BMR
    3. Tachycardia
    4. Dry and coarse skin
(Ref. 1, p. 565)
  1. Mental retardation can occur in:
    1. Cretinism
    2. Juvenile myxoedema
    3. Myxoedema
    4. Juvenile thyrotoxicosis
(Ref. 1, p. 565)
69 D
70 C
71 D
72 D
73 A
74 D
75 C
76 A
281
  1. Parathyroid hormone (PTH) is synthesised in:
    1. Chief cells of parathyroid glands
    2. Oxyphil cells of parathyroid glands
    3. Para follicular cells of thyroid gland
    4. Follicular cells of thyroid gland
(Ref. 1, p. 569)
  1. The number of amino acid residues in PTH is:
    1. 51
    2. 84
    3. 90
    4. 115
(Ref. 1, p. 568)
  1. Amino acid residues which are essential for the biological activity of PTH are:
    1. N-terminal 34 amino acids
    2. N-terminal 50 amino acids
    3. C-terminal 34 amino acids
    4. C-terminal 50 amino acids
(Ref. 1, p. 568)
  1. Half-life of PTH is:
    1. A few seconds
    2. A few minutes
    3. A few hours
    4. A few days
(Ref. 1, p. 569)
  1. The second messenger for PTH is:
    1. Cyclic AMP
    2. Cyclic GMP
    3. Diacylglycerol
    4. Inositol triphosphate
(Ref. 1, p. 570)
  1. PTH causes all of the following except:
    1. Increased intestinal absorption of calcium
    2. Increased intestinal absorption of phosphate
    3. Increased tubular reabsorption of calcium
    4. Increased tubular reabsorption of phosphate
(Ref. 1, p. 570)
  1. Secretion of PTH is regulated by:
    1. Hypothalamus
    2. Anterior pituitary
    3. Feedback effect of plasma PTH
    4. Feedback effect of plasma calcium
(Ref. 1, p. 570)
77 A
78 B
79 A
80 B
81 A
82 D
83 D
282
  1. A high concentration of PTH in blood causes:
    1. Increase in plasma calcium and inorganic phosphorus
    2. Decrease in plasma calcium and inorganic phosphorus
    3. Increase in plasma calcium and decrease in plasma inorganic phosphorus
    4. Decrease in plasma calcium and increase in plasma inorganic phosphorus
(Ref. 1, p. 571)
  1. Tetany can occur:
    1. In primary hyperparathyroidism
    2. In secondary hyperparathyroidism
    3. In idiopathic hypoparathyroidism
    4. After accidental removal of parathyroid glands
(Ref. 1, p. 571)
  1. In hypoparathyroidism:
    1. Plasma calcium and inorganic phosphorus are low
    2. Plasma calcium and inorganic phosphorus are high
    3. Plasma calcium is low and inorganic phosphorus high
    4. Plasma calcium is high and inorganic phosphorus low
(Ref. 1, p. 571)
  1. The number of amino acid residues in calcitonin is:
    1. 9
    2. 32
    3. 51
    4. 84
(Ref. 1, p. 574)
  1. Calcitonin is synthesised in:
    1. Parathyroid glands
    2. Thyroid gland
    3. Pars intermedia of pituitary
    4. Adrenal cortex
(Ref. 1, p. 574)
  1. Plasma calcium is influenced by all of the following except:
    1. Parathormone
    2. Aldosterone
    3. Calcitonin
    4. Calcitriol
(Ref. 1, p. 574)
84 C
85 D
86 C
87 B
88 B
89 B
283
  1. α Cells of islets of Langerhans secrete:
    1. Insulin
    2. Glucagon
    3. Somatostatin
    4. Cholecystokinin
(Ref. 1, p. 611)
  1. Insulin is secreted by following cells of islets of Langerhans:
    1. α cells
    2. β cells
    3. δ cells
    4. F cells
(Ref. 1, p. 611)
  1. Insulin is made up of:
    1. A single polypeptide chain having 51 amino acid residues
    2. A single polypeptide chain having 84 amino acid residues
    3. A-chain having 21 and B-chain having 30 amino acid residues
    4. A-chain having 30 and B-chain having 21 amino acid residues
(Ref. 1, p. 611)
  1. The number of amino acid residues in proinsulin is:
    1. 51
    2. 64
    3. 78-86
    4. 119
(Ref. 1, p. 613)
  1. Pre-proinsulin contains a leader sequence having:
    1. 9 amino acid residues
    2. 23 amino acid residues
    3. 27 amino acid residues
    4. 33 amino acid residues
(Ref. 1, p. 612)
  1. The number of intra-chain disulphide bonds in proinsulin is:
    1. One
    2. Two
    3. Three
    4. Four
(Ref. 1, p. 613)
  1. Crystallisation of insulin occurs in the presence of:
    1. Chromium
    2. Copper
    3. Zinc
    4. Calcium
(Ref. 1, p. 612)
90 B
91 B
92 C
93 C
94 B
95 C
96 C
284
  1. Daily secretion of insulin is about:
    1. 10-20 mg
    2. 40-50 mg
    3. 10-20 units
    4. 40-50 units
(Ref. 1, p. 614)
  1. Insulin receptors are decreased in number in:
    1. Obesity
    2. Starvation
    3. Hyperinsulinism
    4. Kwashiorkor
(Ref. 1, p. 619)
  1. Insulin binding sites are present on the:
    1. α-subunits of insulin receptor
    2. β-subunits of insulin receptor
    3. γ-subunits of insulin receptor
    4. α-and β-subunits of insulin receptor
(Ref. 1, p. 617)
  1. α-Subunits of insulin receptor are present:
    1. Outside the cell membrane
    2. In the cell membrane
    3. Across the cell membrane
    4. In the cytosol
(Ref. 1, p. 617)
  1. β-Subunits of insulin receptor are present:
    1. Outside the cell membrane
    2. In the cell membrane
    3. Across the cell membrane
    4. In the cytosol
(Ref. 1, p. 617)
  1. In the insulin receptor, tyrosine kinase domain is present in:
    1. α-Subunits
    2. β-Subunits
    3. γ-Subunits
    4. δ-Subunits
(Ref. 1, p. 617)
  1. Binding of insulin to its receptor activates:
    1. Adenylate cyclase
    2. Guanylate cyclase
    3. Phospholipase C
    4. Tyrosine kinase
(Ref. 1, p. 620)
97 D
98 A
99 A
100 A
101 C
102 B
103 D
285
  1. Insulin receptor is made up of:
    1. One α-and one β-subunit
    2. Two α-and two β-subunits
    3. Two α-, two β and two γ-subunits
    4. One α-, one β-, one γ-and one δ-subunits
(Ref. 1, p. 617)
  1. Insulin receptor has:
    1. Insulin binding site
    2. Tyrosine kinase domain
    3. Autophosphorylation site
    4. All of the above
(Ref. 1, p. 617)
  1. Insulin decreases:
    1. Glycogenesis
    2. Glycolysis
    3. Gluconeogenesis
    4. Tubular reabsorption of glucose
(Ref. 1, p. 616)
  1. Insulin increases:
    1. Glycogenesis
    2. Gluconeogenesis
    3. Lipolysis
    4. Blood glucose
(Ref. 1, pp. 616-617)
  1. Insulin increases:
    1. Protein synthesis
    2. Fatty acid synthesis
    3. Glycogen synthesis
    4. All of the above
(Ref. 1, pp. 616-617)
  1. Insulin decreases the synthesis of:
    1. Hexokinase
    2. Glucokinase
    3. PEP carboxykinase
    4. Glycogen synthetase
(Ref. 1, p. 616)
  1. Diabetes mellitus can occur due to all of the following except:
    1. Deficient insulin secretion
    2. Tumour of β cells
    3. Decrease in number of insulin receptors
    4. Formation of insulin antibodies
(Ref. 1, p. 622)
104 B
105 D
106 C
107 A
108 D
109 C
110 B
286
  1. Hypoglycaemic coma can occur:
    1. In untreated diabetes mellitus
    2. In starvation
    3. After overdose of oral hypoglycaemic drugs
    4. After overdose of insulin
(Ref. 1, p. 217)
  1. Second messenger for glucagon is:
    1. Cyclic AMP
    2. Diacylglycerol
    3. Cyclic GMP
    4. Inositol triphosphate
(Ref. 1, p. 624)
  1. Number of amino acid residues in glucagon is:
    1. 29
    2. 34
    3. 51
    4. 84
(Ref. 1, p. 623)
  1. Glucagon secretion increases:
    1. After a carbohydrate-rich meal
    2. After a fat-rich meal
    3. When blood glucose is high
    4. When blood glucose is low
(Ref. 1, p. 216)
  1. The main effect of glucagon is to increase:
    1. Glycolysis in muscles
    2. Glycogenolysis in muscles
    3. Glycogenolysis in liver
    4. Glycogenesis in liver
(Ref. 1, p. 624)
  1. Tyrosine is required for the synthesis of all of the following except:
    1. Melatonin
    2. Epinephrine
    3. Norepinephrine
    4. Thyroxine
(Ref. 1, pp. 352-354)
  1. Dopamine is synthesised from:
    1. Dihydroxyphenylalanine
    2. Epinephrine
    3. Norepinephrine
    4. Metanephrine
(Ref. 1, pp. 355-356)
  1. Blood brain barrier can be crossed by:
    1. Epinephrine
    2. Dopamine
    3. Dopa
    4. All of the above
(Ref. 1, p. 589)
111 D
112 A
113 A
114 D
115 C
116 A
117 A
118 C
287
  1. Epinephrine is synthesised in:
    1. Chromaffin cells of adrenal medulla
    2. Sympathetic ganglia
    3. Brain
    4. All of the above
(Ref. 1, p. 588)
  1. Immediate precursor of epinephrine is:
    1. Metanephrine
    2. Norepinephrine
    3. Dopa
    4. Dopamine
(Ref. 1, p. 589)
  1. The chief metabolite of catecholamines is:
    1. Metanephrine
    2. Normetanephrine
    3. 3,4-Dihydroxymandelic acid
    4. Vanillylmandelic acid
(Ref. 1, p. 591)
  1. An enzyme involved in catabolism of catecholamines is:
    1. Dopa decarboxylase
    2. Aromatic amino acid decarboxylase
    3. Monoamine oxidase
    4. Catechol oxidase
(Ref. 1, p. 591)
  1. Norepinephrine binds mainly to:
    1. α-Adrenergic receptors
    2. β-Adrenergic receptors
    3. Muscarinic receptors
    4. Nicotinic receptors
(Ref. 1, p. 592)
  1. A stimulatory G-protein transduces the signals from:
    1. α1-and β1-adrenergic receptors
    2. α2-and β2-adrenergic receptors
    3. α1-and α2-adrenergic receptors
    4. β1-and β2-adrenergic receptors
(Ref. 1, p. 592)
  1. Binding of catecholamines to α2 - adrenergic 2 receptors:
    1. Increases the intracellular concentration of cAMP
    2. Increases the intracellular concentration of cGMP
    3. Decreases the intracellular concentration of cAMP
    4. Decreases the intracellular concentration of cGMP
(Ref. 1, p. 592)
119 D
120 B
121 D
122 C
123 A
124 D
125 C
288
  1. Phosphoinositide cascade is activated on binding of catecholamines to:
    1. α1-Adrenergic receptors
    2. α2-Adrenergic receptors
    3. β1-Adrenergic receptors
    4. β2-Adrenergic receptors
(Ref. 1, p. 543)
  1. Epinephrine decreases:
    1. Glycogenesis
    2. Glycogenolysis
    3. Gluconeogenesis
    4. Lipolysis
(Ref. 1, pp. 204, 592)
  1. Epinephrine increases the concentration of free fatty acids in plasma by increasing:
    1. Extramitochondrial fatty acid synthesis
    2. Mitochondrial fatty acid chain elongation
    3. Microsomal fatty acid chain elongation
    4. Lipolysis in adipose tissue
(Ref. 1, p. 592)
  1. Epinephrine increases all of the following except:
    1. Glycogenolysis in muscles
    2. Lipolysis in adipose tissue
    3. Gluconeogenesis in muscles
    4. Glucagon secretion
(Ref. 1, p. 592)
  1. Secretion of catecholamines is increased in:
    1. Cushing's syndrome
    2. Addison's disease
    3. Phaeochromocytoma
    4. Simmond's disease
(Ref. 1, p. 592)
  1. Zona glomerulosa of adrenal cortex synthesises:
    1. Glucocorticoids
    2. Mineralocorticoids
    3. Androgens
    4. Estrogen and progesterone
(Ref. 1, p. 575)
  1. Cortisol is a:
    1. Glucocorticoid
    2. Mineralocorticoid
    3. Androgen
    4. Estrogen
(Ref. 1, p. 575)
126 A
127 A
128 D
129 C
130 C
131 B
132 A
289
  1. The major mineralocorticoid is:
    1. Hydrocortisone
    2. Aldosterone
    3. Aldactone A
    4. Androstenedione
(Ref. 1, p. 575)
  1. Steroid hormones are synthesised in all of the following except:
    1. Testes
    2. Ovaries
    3. Adrenal medulla
    4. Adrenal cortex
(Ref. 1, pp. 575, 588. 594)
  1. Steroid hormones are synthesised from:
    1. Cholesterol
    2. 7-Dehydrocholesterol
    3. Calcitriol
    4. 7-Hydroxycholesterol
(Ref. 1, p. 576)
  1. A common intermediate in the synthesis of all the steroid hormones is:
    1. Pregnenolone
    2. 17-Hydroxypregnenolone
    3. Corticosterone
    4. Progesterone
(Ref. 1, p. 576)
  1. A common intermediate in the synthesis of cortisol and aldosterone is:
    1. Progesterone
    2. Testosterone
    3. Estradiol
    4. None of the above
(Ref. 1, p. 579)
  1. A common intermediate in the synthesis of estrogens is:
    1. Cortisol
    2. Androstenedione
    3. Corticosterone
    4. 11-Deoxycorticosterone
(Ref. 1, p. 600)
  1. Glucocorticoids are transported in blood:
    1. In association with transcortin chiefly
    2. In association with albumin to some extent
    3. In free form partly
    4. All of the above forms
(Ref. 1, p. 580)
133 B
134 C
135 A
136 A
137 A
138 B
139 D
290
  1. All the following statements about transcortin are true except:
    1. It is synthesised in liver
    2. It transports glucocorticoids
    3. It transports aldosterone
    4. It transports progesterone
(Ref. 1, p. 580)
  1. The second messenger for glucocorticoids is:
    1. Cyclic AMP
    2. Cyclic GMP
    3. Inositol triphosphate
    4. No second messenger is required
(Ref. 1, pp. 583-584)
  1. Glucocorticoids increase all of the following except:
    1. Gluconeogenesis
    2. Lipolysis in extremities
    3. Synthesis of eicosanoids
    4. Hepatic glycogenesis
(Ref. 1, p. 582)
  1. Glucocorticoids increase the synthesis of all of the following except:
    1. Glucokinase
    2. Glucose-6-phosphatase
    3. Fructose-1, 6-biphosphatase
    4. Pyruvate carboxylase
(Ref. 1, p. 212)
  1. Secretion of glucocorticoids is regulated by all the following except:
    1. Hypothalamus
    2. Anterior pituitary
    3. Feedback control by blood glucose
    4. Feedback control by glucocorticoids
(Ref. 1, pp. 550-551, 580)
  1. Excessive secretion of glucocorticoids raises blood glucose by:
    1. Decreasing glycogenesis
    2. Increasing glycogenolysis
    3. Increasing gluconeogenesis
    4. Inhibiting HMP shunt
(Ref. 1, p. 216)
140 C
141 D
142 C
143 A
144 C
145 C
291
  1. Mineralocorticoids regulate the metabolism of all of the following except:
    1. Sodium
    2. Potassium
    3. Calcium
    4. Chloride
(Ref. 5, pp. 772-773)
  1. Mineralocorticoids increase the tubular reabsorption of:
    1. Sodium and calcium
    2. Sodium and potassium
    3. Sodium and chloride
    4. Potassium and chloride
(Ref. 5, pp. 772-773)
  1. Mineralocorticoids increase the tubular secretion of:
    1. Sodium
    2. Potassium
    3. Chloride
    4. Bicarbonate
(Ref. 1, p. 582)
  1. Secretion of mineralocorticoids is increased by:
    1. ACTH
    2. Angiotensin
    3. Hypokalaemia
    4. Hypernatraemia
(Ref. 1, p. 582)
  1. In Addison's disease, there is excessive retention of:
    1. Potassium
    2. Sodium
    3. Chloride
    4. Water
(Ref. 1, p. 586)
  1. In adrenogenital syndrome due to total absence of 21-hydroxylase in adrenal cortex, there is:
    1. Deficient secretion of glucocorticoids
    2. Deficient secretion of mineralocorticoids
    3. Excessive secretion of androgens
    4. All of the above
(Ref. 1, p. 587)
  1. Spironolactone is an antagonist of:
    1. Cortisol
    2. Hydrocortisone
    3. Aldosterone
    4. Testosterone
(Ref. 5, p. 778)
146 C
147 C
148 B
149 B
150 A
151 D
152 C
292
  1. Androgens are synthesised in:
    1. Leydig cells in testes
    2. Sertoli cells in testes
    3. Seminiferous tubules
    4. Prostate gland
(Ref. 1, p. 594)
  1. Testosterone is transported in blood by:
    1. Transcortin
    2. Testosterone binding globulin
    3. Testosterone estrogen binding globulin
    4. Albumin
(Ref. 1,pp. 596-597)
  1. The metabolites of androgens are:
    1. 17-Hydroxysteroids
    2. 17-Ketosteroids
    3. 11-Hydroxysteroids
    4. 11-Ketosteroids
(Ref. 1, p. 598)
  1. An androgen which is more powerful than testosterone is:
    1. Androstenedione
    2. Dihydrotestosterone
    3. Androsterone
    4. Epiandrosterone
(Ref. 1, p. 597)
  1. Secretion of androgens is increased by:
    1. LH
    2. FSH
    3. ACTH
    4. Growth hormone
(Ref. 1, p. 598)
  1. During late pregnancy, the major source of progesterone is:
    1. Adrenal cortex
    2. Placenta
    3. Corpus luteum
    4. Graafian follicles
(Ref. 1, p. 604)
  1. Progesterone is transported in blood by:
    1. Transcortin
    2. Sex hormone binding globulin
    3. Albumin
    4. Testosterone estrogen binding globulin
(Ref. 1, pp. 580, 601)
153 A
154 C
155 B
156 B
157 A
158 B
159 A
293
  1. The major metabolite of progesterone is:
    1. Pregnenolone
    2. Pregnanediol
    3. Estradiol
    4. Norethindrone
(Ref. 1, pp. 601-602)
  1. Secretion of progesterone:
    1. Is more in first half of menstrual cycle than in second half
    2. Is more in second half of menstrual cycle than in first half
    3. Remains constant during menstrual cycle
    4. Decreases during pregnancy
(Ref. 1, pp. 603-604)
  1. Women become susceptible to osteoporosis after menopause due to decreased:
    1. Secretion of parathormone
    2. Conversion of vitamin D into calcitriol
    3. Secretion of estrogen
    4. Secretion of progesterone
(Ref. 1, p. 606)
  1. A hormone used for detection of pregnancy is:
    1. Estrogen
    2. Progesterone
    3. Oxytocin
    4. Chorionic gonadotropin
(Ref. 1, p. 604)
  1. Placenta secretes all of the following except:
    1. FSH
    2. Progesterone
    3. Estrogen
    4. Chorionic gonadotropin
(Ref. 1, p. 604)
  1. Gastrin is a polypeptide made up of:
    1. Five amino acids
    2. Twelve amino acids
    3. Seventeen amino acids
    4. Twenty amino acids
(Ref. 5, p. 804)
  1. Biological activity of gastrin is present in the:
    1. Four N-terminal amino acids
    2. Four C-terminal amino acids
    3. Five N-terminal amino acids
    4. Five C-terminal amino acids
(Ref. 5, p. 804)
160 B
161 B
162 C
163 D
164 A
165 C
166 B
294
  1. Pentagastrin is a:
    1. Naturally occurring form of gastrin
    2. Inactive metabolite of gastrin
    3. Active metabolite of gastrin
    4. Synthetic form of gastrin
(Ref. 5, p. 804)
  1. Secretion of gastrin is evoked by:
    1. Entry of food into stomach
    2. Vagal stimulation
    3. Lower aliphatic alcohols
    4. All of the above
(Ref. 5, p. 804)
  1. Gastrin stimulates:
    1. Gastric motility
    2. Gastric secretion
    3. Both of the above
    4. Neither of the above
(Ref. 5, p. 805)
  1. Secretin is made up of:
    1. 17 amino acids
    2. 27 amino acids
    3. 37 amino acids
    4. 47 amino acids
(Ref. 5, p. 802)
  1. Secretin causes all of the following except:
    1. Secretion of pancreatic juice
    2. Secretion of bile
    3. Inhibition of gastric secretion
    4. Stimulation of intestinal motility
(Ref. 5, pp. 802-803)
  1. All the following statements about cholecystokinin-pancreozymin are true except:
    1. It is secreted by mucosa of small intestine
    2. It stimulates secretion of pancreatic juice rich in enzymes
    3. It stimulates contraction of gall bladder
    4. It inhibits gastric motility
(Ref. 5, p. 806)
  1. All the following statements about pancreatic somatostatin are true except:
    1. It is secreted by δ cells of islets of Langerhans
    2. It stimulates the secretion of gastrin
    3. It inhibits the secretion of secretin
    4. It inhibits the secretion of cholecystokinin-pancreozymin
(Ref. 5, p. 807)
167 D
168 D
169 C
170 B
171 D
172 D
173 B
295
  1. Histidine is converted into histamine by:
    1. Carboxylation
    2. Decarboxylation
    3. Methylation
    4. Hydroxylation
(Ref. 1, p. 349)
  1. Histamine is synthesised in:
    1. Brain
    2. Mast cells
    3. Basophils
    4. All of the above
(Ref. 5, p. 585)
  1. Histamine causes all the following except:
    1. Stimulation of gastric secretion
    2. Vasoconstriction
    3. Pruritus
    4. Increase in capillary permeability
(Ref. 5, p. 585)
  1. H2-receptors are blocked by:
    1. Diphenhydramine
    2. Mepayramine
    3. Pyrilamine
    4. Cimetidine
(Ref. 5, p. 586)
  1. Serotonin is synthesised from:
    1. Serine
    2. Phenylalanine
    3. Tyrosine
    4. Tryptophan
(Ref. 1, p. 352)
  1. All the following statements about serotonin are true except:
    1. It causes vasodilatation
    2. It causes bronchoconstriction
    3. It is metabolised by monoamine oxidase
    4. Its metabolite is 5-hydroxyindole acetic acid
(Ref. 1, p. 352)
  1. All the following statements about angiotensin are true except:
    1. Its precursor is an α2-globulin
    2. Its active form is an octapeptide
    3. It is a vasodilator
    4. It increases the secretion of aldosterone
(Ref. 1, pp. 581-582)
174 B
175 D
176 B
177 D
178 D
179 A
180 C
296
  1. Methyl dopa decreases blood pressure by:
    1. Inhibiting the synthesis of catecholamines
    2. Antagonising the action of aldosterone
    3. Stimulating the release of renin
    4. Inhibiting the breakdown of angiotensin
(Ref. 1, p. 589)
  1. Binding of gamma-aminobutyric acid to its receptors in brain increases the permeability of cell membrane to:
    1. Cl-
    2. Na+
    3. K+
    4. Ca++
(Ref. 2, p. 309)
  1. Binding of acetylcholine to its receptors increases the permeability of cell membrane to:
    1. Ca++
    2. Na+
    3. K+
    4. Na+ and K+
(Ref. 1, p. 831)
  1. All the following statements about β-endorphin are true except:
    1. It is a polypeptide
    2. Its precursor is pro-opio-melanocortin
    3. Its receptors are present in brain
    4. Its action is blocked by morphine
(Ref. 5, p. 715)
  1. All the following statements about epidermal growth factor are true except:
    1. It is a protein
    2. It possesses quaternary structure
    3. Its receptor is made up of a single polypeptide chain
    4. Its receptor possesses tyrosine kinase domain
(Ref. 2, p. 351)
  1. Met-enkephalin is a:
    1. Tripeptide
    2. Pentapeptide
    3. Octapeptide
    4. Decapeptide
(Ref. 5, p. 715)
  1. Vasoconstrictor effect of ADH is mediated by:
    1. cAMP
    2. cGMP
    3. Protein kinase C
    4. Angiotensin II
(Ref. 1, p. 559)
181 A
182 A
183 D
184 D
185 B
186 B
187 C
297
  1. The rate limiting step in catecholamine synthesis is catalysed by:
    1. Phenylalanine hydroxylase
    2. Tyrosine hydroxylase
    3. Dopa decarboxylase
    4. Phenylethanolamine N-methyl transferase
(Ref. 1, p. 588)
  1. Dopa decarboxylase is inhibited by:
    1. Epinephrine
    2. Norepinephrine
    3. α-Methyldopa
    4. None of the above
(Ref. 1, p. 589)
  1. Tyrosine hydroxylase is inhibited by:
    1. Catecholamines
    2. α-Methyldopa
    3. Phenylalanine
    4. Vanillyl mandelic acid
(Ref. 1, p. 589)
  1. Urinary excretion of vanillyl mandelic acid is increased in:
    1. Phaeochromocytoma
    2. Cushing's syndrome
    3. Carcinoid syndrome
    4. Aldosteronism
(Ref. 1, p. 591)
  1. Iodide uptake by thyroid gland is decreased by:
    1. Thiocyanate
    2. Thiouracil
    3. Thiourea
    4. Methimazole
(Ref. 1, p. 562)
  1. Binding of growth hormone to its receptor results in phosphorylation of:
    1. JAK-2
    2. Growth hormone receptor
    3. STATs
    4. All of the above
(Ref. 1, p. 552)
  1. Binding of growth hormone to its receptor results in increased transcription of:
    1. c-fos gene
    2. c-myc gene
    3. p 53 gene
    4. None of the above
(Ref. 1, p. 553)
188 B
189 C
190 A
191 A
192 A
193 D
194 A
298
  1. Activation of IRS-1, PI-3 kinase and GRB-2 is brought about by:
    1. Glucagon
    2. Insulin
    3. Prolactin
    4. IGF-2
(Ref. 1, pp. 620-621)
  1. The protein IRS-1 is phosphorylated by:
    1. Protein kinase A
    2. Protein kinase C
    3. Tyrosine kinase activity of insulin receptor
    4. Tyrosine kinase activity of IGF-1 receptor
(Ref. 1, p. 620)
  1. Phosphorylated IRS-1 activates GRB-2 which is:
    1. G-protein receptor binding protein-2
    2. Growth factor receptor binding protein-2
    3. Growth hormone receptor binding protein-2
    4. Glucocorticoid receptor binding protein-2
(Ref. 1, p. 620)
  1. STAT proteins are:
    1. Thermostat proteins of brain
    2. Glucostat proteins of hepatocyte cell membrane
    3. Short term activators of translation
    4. Signal transduction and activators of transcription
(Ref. 1, p. 547)
  1. Activated phospholipase C acts on:
    1. Phosphatidyl inositol-4, 5-biphosphate
    2. Inositol-1, 4, 5-triphosphate
    3. Protein kinase C
    4. Pl-3 kinase
(Ref. 1, p. 546)
  1. Phospholipase C is activated by:
    1. Gs proteins
    2. Gi proteins
    3. Gq proteins
    4. G12 proteins
(Ref. 1, p. 543)
195 B
196 C
197 A
198 A
199 A
200 D

Proteoglycans and Glycoproteins24

  1. Proteoglycans are made up of proteins and:
    1. Glucosamine
    2. Mannosamine
    3. Sialic acid
    4. Mucopolysaccharides
(Ref. 1, p. 695)
  1. All of the following are glycoproteins except:
    1. Collagen
    2. Albumin
    3. Transferrin
    4. IgM
(Ref. 1, p. 675)
  1. Sialic acids are present in:
    1. Proteoglycans
    2. Glycoproteins
    3. Both of the above
    4. Neither of the above
(Ref. 1, pp. 677, 701)
  1. Hyaluronidase hydrolyses:
    1. Hyaluronic acid
    2. Chondroitin sulphate
    3. Heparin
    4. Hyaluronic acid and chondroitin sulphate
(Ref. 1, p. 706)
  1. The most abundant protein in bones is:
    1. Collagen type I
    2. Collagen type II
    3. Collagen type III
    4. Non-collagen proteins
(Ref. 1, p. 696)
  1. The most abundant collagen in cartilages is:
    1. Type I
    2. Type II
    3. Type III
    4. Type IV
(Ref. 1, p. 696)
1 D
2 B
3 B
4 D
5 A
6 B
300
  1. Collagen and elastin have the following similarity:
    1. Both are triple helices
    2. Both have hydroxyproline residues
    3. Both have hydrolysine residues
    4. Both are glycoproteins
(Ref. 1, pp. 698-699)
  1. Abnormal collagen structure is seen in all of the following except:
    1. I-cell disease
    2. Osteogenesis imperfecta
    3. Menkes' disease
    4. Ehlers-Danlos syndrome
(Ref. 1, pp. 691, 698)
  1. I-cell disease results from absence of the following from lysosomal enzymes:
    1. Signal sequence
    2. Mannose-6-phosphate
    3. Sialic acid
    4. A serine residue
(Ref. 1, p. 691)
  1. In I-cell disease, lysosomal enzymes:
    1. Are not synthesised
    2. Are inactive
    3. Lack signal sequence
    4. Cannot reach lysosomes
(Ref. 1, p. 691)
  1. The following is present as a marker in lysosomal enzymes to direct them to their destination:
    1. Glucose-6-phosphate
    2. Mannose-6-phosphate
    3. Galactose-6-phosphate
    4. N-Acetyl neuraminic acid
(Ref. 1, p. 691)
  1. Marfan's syndrome results from a mutation in the gene encoding:
    1. Collagen
    2. Elastin
    3. Fibrillin
    4. Keratin
(Ref. 1, p. 699)
7 B
8 A
9 B
10 D
11 B
12 C
301
  1. All the following statements about fibronectin are true except:
    1. It is a glycoprotein
    2. It is a triple helix
    3. It is present in extracellular matrix
    4. It binds with integrin receptors of cell
(Ref. 1, p. 700)
  1. Fibronectin has binding sites for all of the following except:
    1. Glycophorin
    2. Collagen
    3. Heparin
    4. Integrin receptor
(Ref. 1, p. 700)
  1. Fibronectin is involved in:
    1. Cell adhesion
    2. Cell movement
    3. Both of the above
    4. Neither of the above
(Ref. 1, p. 701)
  1. Glycoproteins are marked for destruction by removal of their:
    1. Oligosaccharide prosthetic groups
    2. Sialic acid residues
    3. Mannose residues
    4. N-terminal amino acids
(Ref. 1, p. 678)
  1. Asialoglycoprotein receptors are present in cell membranes of:
    1. Erythrocytes
    2. Platelets
    3. Neutrophils
    4. Liver
(Ref. 1, p. 678)
  1. Glycophorin is present in cell membranes of:
    1. Erythrocytes
    2. Platelets
    3. Neutrophils
    4. Liver
(Ref. 1, p. 769)
  1. Selectins are proteins that can recognise specific:
    1. Carbohydrates
    2. Lipids
    3. Amino acids
    4. Nucleotides
(Ref. 1, pp. 678-679)
  1. Hunter's syndrome results from absence of:
    1. Hexosaminidase A
    2. Iduronate sulphatase
    3. Neuraminidase
    4. Arylsulphatase B
(Ref. 1, p. 705)
13 B
14 A
15 C
16 B
17 D
18 A
19 A
20 B

Biochemistry of Cancer25

  1. A cancer cell is characterised by:
    1. Uncontrolled cell division
    2. Invasion of neighbouring cells
    3. Spread to distant sites
    4. All of the above
(Ref. 1, p. 787)
  1. If DNA of a cancer cell is introduced into a normal cell, the recipient cell:
    1. Destroys the DNA
    2. Loses its ability to divide
    3. Dies
    4. Changes into a cancer cell
(Ref. 1, p. 790)
  1. A normal cell can be transformed into a cancer cell by all of the following except:
    1. Ionising radiation
    2. Mutagenic chemicals
    3. Oncogenic bacteria
    4. Some viruses
(Ref. 1, pp. 786-787, 790)
  1. Proto-oncogenes are present in:
    1. Oncoviruses
    2. Cancer cells
    3. Healthy human cells
    4. Prokaryotes
(Ref. 1, p. 792)
1 D
2 D
3 C
4 C
303
  1. All the following statements about proto-oncogenes are true except:
    1. They are present in human beings
    2. They are present in healthy cells
    3. Proteins encoded by them are essential
    4. They are expressed only when a healthy cell has been transformed into a cancer cell
(Ref. 1, p. 792)
  1. Various oncogenes may encode all of the following except:
    1. Carcinogens
    2. Growth factors
    3. Receptors for growth factors
    4. Signal transducers for growth factors
(Ref. 1, p. 797)
  1. ras proto-oncogene is converted into oncogene by:
    1. A point mutation
    2. Chromosomal translocation
    3. Insertion of a viral promoter upstream of the gene
    4. Gene amplification
(Ref. 1, p. 795)
  1. ras proto-oncogene encodes:
    1. Epidermal growth factor (EGF)
    2. Receptor for EGF
    3. Signal transducer for EGF
    4. Nuclear transcription factor
(Ref. 2, p. 356)
  1. p 53 gene is:
    1. A proto-oncogene
    2. An oncogene
    3. A tumour suppressor gene
    4. None of the above
(Ref. 1, p. 800)
  1. Retinoblastoma can result from a mutation in:
    1. ras proto-oncogene
    2. erbB proto-oncogene
    3. p 53 gene
    4. RB 1 gene
(Ref. 1, pp. 799-800)
5 D
6 A
7 A
8 C
9 C
10 D
304
  1. All the following statements about retinoblastoma are true except:
    1. At least two mutations are required for its development
    2. One mutation can be inherited from a parent
    3. Children who have inherited one mutation develop retinoblastoma at a younger age
    4. RB 1 gene promotes the development of retinoblastoma
(Ref. 1, pp. 799-800)
  1. Ames' assay is a rapid method for detection of:
    1. Oncoviruses
    2. Retroviruses
    3. Chemical carcinogens
    4. Typhoid
(Ref. 1, p. 789)
  1. Amplification of dihydrofolate reductase gene in a cancer cell makes the cell:
    1. Susceptible to folic acid deficiency
    2. Less malignant
    3. Resistant to amethopterin therapy
    4. Responsive to amethopterin therapy
(Ref. 1, p. 795)
  1. Conversion of a procarcinogen into a carcinogen often requires:
    1. Proteolysis
    2. Microsomal hydroxylation
    3. Exposure to ultraviolet radiation
    4. Exposure to X-rays
(Ref. 2, p. 704)
  1. The only correct statement about oncoviruses is:
    1. All the oncoviruses are RNA viruses
    2. Reverse transcriptase is present in all oncoviruses
    3. Viral oncogenes are identical to human protooncogenes
    4. Both DNA and RNA viruses can be oncoviruses
(Ref. 1, p. 790)
11 D
12 C
13 C
14 B
15 D
305
  1. RB 1 gene is:
    1. A tumour suppressor gene
    2. Oncogene
    3. Proto-oncogene
    4. Activated proto-oncogene
(Ref. 1, p. 799)
  1. Cancer cells may become resistant to amethopterin by:
    1. Developing mechanisms to destroy amethopterin
    2. Amplification of dihydrofolate reductase gene
    3. Mutation in the dihydrofolate reductase gene so that the enzyme is no longer inhibited by amethopterin
    4. Developing alternate pathway of thymidylate synthesis
(Ref. 1, p. 795)
  1. In Ames' assay, a special strain of S. typhimurium is used which lacks the ability to synthesise:
    1. Histidine
    2. Arginine
    3. Lysine
    4. Threonine
(Ref. 1, p. 789)
  1. In Ames' assay, addition of a carcinogen to the culture medium allows S. typhimurium to grow:
    1. In the presence of histidine
    2. In the presence of arginine
    3. In the absence of histidine
    4. In the absence of arginine
(Ref. 1, p. 789)
  1. InAmes' assay, the chemical under test is pre-incubated with liver homogenate because:
    1. It converts pro-carcinogens into carcinogens
    2. Liver can metabolise histidine
    3. Salmonella mainly infects liver
    4. Liver is very susceptible to cancer
(Ref. 1, p. 789)
16 A
17 B
18 A
19 C
20 A

Tests for Liver, Kidney, Thyroid and Pancreatic Functions26

  1. Bile pigments are present and urobilinogen absent in urine in:
    1. Haemolytic jaundice
    2. Hepatocellular jaundice
    3. Obstructive jaundice
    4. Crigler-Najjar syndrome
(Ref. 1, p. 372)
  1. Bile pigments are absent and urobilinogen increased in urine in:
    1. Haemolytic jaundice
    2. Hepatocellular jaundice
    3. Obstructive jaundice
    4. Rotor's syndrome
(Ref. 1, p. 372)
  1. In obstructive jaundice, urine shows:
    1. Absence of bile pigments and urobilinogen
    2. Presence of bile pigments and urobilinogen
    3. Absence of bile pigments and presence of urobilinogen
    4. Presence of bile pigments and absence of urobilinogen
(Ref. 1, p. 372)
1 C
2 A
3 D
307
  1. In haemolytic jaundice, urine shows:
    1. Absence of bile pigments and urobilinogen
    2. Presence of bile pigments and urobilinogen
    3. Absence of bile pigments and presence of urobilinogen
    4. Presence of bile pigments and absence of urobilinogen
(Ref. 1, p. 372)
  1. Serum albumin may be decreased in:
    1. Haemolytic jaundice
    2. Hepatocellular jaundice
    3. Obstructive jaundice
    4. All of the above
(Ref. 1, p. 740)
  1. Normal range of serum albumin is:
    1. 2.0-3.6 gm/dl
    2. 2.0-3.6 mg/dl
    3. 3.5-5.5 gm/dl
    4. 3.5-5.5 mg/dl
(Ref. 1, p. 870)
  1. Normal range of serum globulin is:
    1. 2.0-3.6 mg/dl
    2. 2.0-3.6 gm/dl
    3. 3.5-5.5 mg/dl
    4. 3.5-5.5 gm/dl
(Ref. 1, p. 872)
  1. Serum albumin : globulin ratio is altered in:
    1. Gilbert's disease
    2. Haemolytic jaundice
    3. Viral hepatitis
    4. Stones in bile duct
(Ref. 7, p. 165)
  1. Esterification of cholesterol occurs mainly in:
    1. Adipose tissue
    2. Liver
    3. Muscles
    4. Kidneys
(Ref. 5, p. 961)
  1. Galactose intolerance can occur in:
    1. Haemolytic jaundice
    2. Hepatocellular jaundice
    3. Obstructive jaundice
    4. None of the above
(Ref. 5, p. 958)
  1. Prothrombin is synthesised in:
    1. Erythrocytes
    2. Reticulo-endothelial cells
    3. Liver
    4. Kidneys
(Ref. 1, p. 755)
4 C
5 B
6 C
7 B
8 C
9 B
10 B
11 C
308
  1. Prothrombin time remains prolonged even after parenteral administration of vitamin K in:
    1. Haemolytic jaundice
    2. Liver damage
    3. Biliary obstruction
    4. Steatorrhoea
(Ref. 5, p. 964)
  1. All the following statements about obstructive jaundice are true except:
    1. Conjugated bilirubin in serum is normal
    2. Total bilirubin in serum is raised
    3. Bile salts are present in urine
    4. Serum alkaline phosphatase is raised
(Ref. 7, pp. 136, 165, 167)
  1. All the following statements about obstructive jaundice are true except:
    1. Prothrombin time may be prolonged due to impaired absorption of vitamin K
    2. Serum alkaline phosphatase may be raised due to increased release of the enzyme from liver cells
    3. Bile salts may enter systemic circulation due to biliary obstruction
    4. There is no defect in conjugation of bilirubin
(Ref. 6, pp. 364, 519)
  1. A test to evaluate detoxifying function of liver is:
    1. Serum albumin: globulin ratio
    2. Galactose tolerance test
    3. Hippuric acid test
    4. Prothrombin time
(Ref. 5, p. 962)
  1. Hippuric acid is formed from:
    1. Benzoic acid and alanine
    2. Benzoic acid and glycine
    3. Glucuronic acid and alanine
    4. Glucuronic acid and glycine
(Ref. 1, p. 347)
12 B
13 A
14 B
15 C
16 B
309
  1. An enzyme which is excreted in urine is:
    1. Lactate dehydrogenase
    2. Amylase
    3. Ornithine transcarbamoylase
    4. None of the above
(Ref. 6, p. 60)
  1. Serum gamma glutamyl transpeptidase is raised in:
    1. Haemolytic jaundice
    2. Myocardial infarction
    3. Alcoholic hepatitis
    4. Acute cholecystitis
(Ref. 6, p. 58)
  1. Oliguria can occur in:
    1. Diabetes mellitus
    2. Diabetes insipidus
    3. Acute glomerulonephritis
    4. Chronic glomerulonephritis
(Ref. 5, p. 1013)
  1. Polyuria can occur in:
    1. Diabetes mellitus
    2. Diarrhoea
    3. Acute glomerulonephritis
    4. High fever
(Ref. 5, p. 1012)
  1. Normal specific gravity of urine is:
    1. 1.000-1.010
    2. 1.012-1.024
    3. 1.025-1.034
    4. 1.035-1.045
(Ref. 7, p. 82)
  1. Specific gravity of urine is raised in all of the following except:
    1. Diabetes mellitus
    2. Diabetes insipidus
    3. Dehydration
    4. Acute glomerulonephritis
(Ref. 7, p. 82)
  1. Specific gravity of urine is decreased in:
    1. Diabetes mellitus
    2. Acute glomerulonephritis
    3. Diarrhoea
    4. Chronic glomerulonephritis
(Ref. 5, p. 1015)
17 B
18 C
19 C
20 A
21 B
22 B
23 D
310
  1. Heavy proteinuria occurs in:
    1. Acute glomerulonephritis
    2. Acute pyelonephritis
    3. Nephrosclerosis
    4. Nephrotic syndrome
(Ref. 5, p. 1030)
  1. Bence-Jones proteinuria occurs in:
    1. Nephrotic syndrome
    2. Renal cancer
    3. Multiple myeloma
    4. Chronic glomerulonephritis
(Ref. 5, p. 117)
  1. Bence-Jones protein precipitates at:
    1. 20 -40 C
    2. 40 -60 C
    3. 60 -80 C
    4. 80 -100 C
(Ref. 5, p. 118)
  1. Renal glycosuria occurs due to:
    1. Increased filtration of glucose in glomeruli
    2. Increased secretion of glucose by renal tubular cells
    3. Decreased reabsorption of glucose by renal tubular cells
    4. Increased conversion of glycogen into glucose in tubular cells
(Ref. 5, p. 429)
  1. Haematuria can occur in:
    1. Haemolytic anaemia
    2. Mismatched blood transfusion
    3. Yellow fever
    4. Stone in urinary tract
(Ref. 7, p. 88)
  1. Haematuria can occur in all of the following except:
    1. Acute glomerulonephritis
    2. Cancer of urinary tract
    3. Stone in urinary tract
    4. Mismatched blood transfusion
(Ref. 7, p. 88)
  1. Chyluria can be detected by addition of the following to the urine:
    1. Sulphosalicylic acid
    2. Nitric acid
    3. Acetic anhydride
    4. Chloroform
(Ref. 7, p. 81)
24 D
25 C
26 B
27 C
28 D
29 D
30 D
311
  1. Normal range of serum urea is:
    1. 0.6-1.5 mg/dl
    2. 9-11 mg/dl
    3. 20-45 mg/dl
    4. 60-100 mg/dl
(Ref. 7, p. 124)
  1. Normal range of serum creatinine is:
    1. 0.6-1.5 mg/dl
    2. 9-11 mg/dl
    3. 20-45 mg/dl
    4. 60-100 mg/dl
(Ref. 7, p. 132)
  1. Standard urea clearance in normal subjects is:
    1. 54 ml/min
    2. 75 ml/min
    3. 110 ml/min
    4. 130 ml/min
(Ref. 5, p. 942)
  1. Maximum urea clearance in normal subjects is:
    1. 54 ml/min
    2. 75 ml/min
    3. 110 ml/min
    4. 130 ml/min
(Ref. 5, p. 942)
  1. Average creatinine clearance in an adult man is about:
    1. 54 ml/min
    2. 75 ml/min
    3. 110 ml/min
    4. 130 ml/min
(Ref. 7, p. 161)
  1. Inulin clearance in an average adult man is about:
    1. 54 ml/min
    2. 75 ml/min
    3. 110 ml/min
    4. 130 ml/min
(Ref. 7, p. 162)
  1. Urea clearance is the:
    1. Amount of urea excreted per minute
    2. Amount of urea present in 100 ml of urine
    3. Volume of blood cleared of urea in one minute
    4. Amount of urea filtered by glomeruli in one minute
(Ref. 5, p. 942)
  1. Inulin clearance is a measure of:
    1. Glomerular filtration rate
    2. Tubular secretion rate
    3. Tubular reabsorption rate
    4. Renal plasma flow
(Ref. 5, p. 944)
31 C
32 A
33 A
34 B
35 C
36 D
37 C
38 A
312
  1. Phenolsulphonephthalein excretion test is an indicator of:
    1. Glomerular filtration
    2. Tubular secretion
    3. Tubular reabsorption
    4. Renal blood flow
(Ref. 5, p. 947)
  1. Para-amino hippurate clearance is an indicator of:
    1. Glomerular filtration
    2. Tubular secretion
    3. Tubular reabsorption
    4. Renal plasma flow
(Ref. 7, p. 163)
  1. Renal plasma flow of an average adult man is:
    1. 120-130 ml/minute
    2. 325-350 ml/minute
    3. 480-520 ml/minute
    4. 560-830 ml/minute
(Ref. 1, p. 871)
  1. Filtration fraction can be calculated from:
    1. Standard urea clearance and PSP excretion
    2. Maximum urea clearance and PSP excretion
    3. Maximum urea clearance and PAH clearance
    4. Inulin clearance and PAH clearance
(Ref. 7, p. 163)
  1. Normal filtration fraction is about:
    1. 0.2
    2. 0.4
    3. 0.6
    4. 0.8
(Ref. 7, p. 163)
  1. Filtration fraction is increased in:
    1. Acute glomerulonephritis
    2. Chronic glomerulonephritis
    3. Hypertension
    4. Hypotension
(Ref. 7, p. 163)
  1. Among the following, a test of glomerular function is:
    1. Urea clearance
    2. PSP excretion test
    3. PAH clearance
    4. Hippuric acid excretion test
(Ref. 7, pp. 161-163)
39 B
40 D
41 D
42 D
43 A
44 C
45 A
313
  1. Among the following, a test of tubular function is:
    1. Creatinine clearance
    2. Inulin clearance
    3. PAH clearance
    4. PSP excretion test
(Ref. 7, pp. 161-163)
  1. A simple way to assess tubular function is to withhold food and water for 12 hours and, then, measure:
    1. Serum urea
    2. Serum creatinine
    3. Urine output in one hour
    4. Specific gravity of urine
(Ref. 7, pp. 162-163)
  1. Among the following, the most sensitive indicator of glomerular function is:
    1. Serum urea
    2. Serum creatinine
    3. Urea clearance
    4. Creatinine clearance
(Ref. 7, pp. 159-161)
  1. All the following statements about inulin are correct except:
    1. It is completely non-toxic
    2. It is completely filtered by glomeruli
    3. It is not reabsorbed by tubular cells
    4. It is secreted by tubular cells
(Ref. 7, p. 161)
  1. Non-protein nitrogenous substances in blood include all of the following except:
    1. Urea
    2. Uric acid
    3. Creatinine
    4. Inositol
(Ref. 7, p. 128)
  1. Non-protein nitrogenous substances in blood are raised in:
    1. Starvation
    2. Liver damage
    3. Renal failure
    4. All of the above
(Ref. 7, pp. 124, 129)
46 D
47 D
48 D
49 D
50 D
51 C
314
  1. Creatinine clearance is decreased in:
    1. Acute tubular necrosis
    2. Acute glomerulonephritis
    3. Hypertension
    4. Myopathies
(Ref. 6, p. 526)
  1. Serum amylase is increased in:
    1. Acute parotitis
    2. Acute pancreatitis
    3. Pancreatic cancer
    4. All of the above
(Ref. 6, p. 523)
  1. Maximum rise in serum amylase occurs in:
    1. Acute parotitis
    2. Acute pancreatitis
    3. Chronic pancreatitis
    4. Pancreatic cancer
(Ref. 6, p. 60)
  1. Serum lipase is increased in:
    1. Acute parotitis
    2. Acute pancreatitis
    3. Infective hepatitis
    4. Biliary obstruction
(Ref. 6, p. 60)
  1. Sweat chlorides are increased in:
    1. Cystic fibrosis
    2. Pancreatic cancer
    3. Acute pancreatitis
    4. None of the above
(Ref. 1, p. 859)
  1. All the following statements about cystic fibrosis are correct except:
    1. It is inherited as an autosomal recessive disease
    2. It affects a number of exocrine glands
    3. It causes increased sweating
    4. Sweat chlorides are above 60 mEq/L in this disease
(Ref. 1, pp. 859-860)
  1. Radioactive iodine uptake by thyroid gland 24 hours after a test dose is:
    1. 1.5-15% of the test dose
    2. 15-20% of the test dose
    3. 20-40% of the test dose
    4. 50-70% of the test dose
(Ref. 5, p. 988)
52 B
53 D
54 B
55 B
56 A
57 C
58 C
315
  1. Radioactive iodine uptake by thyroid gland is increased in:
    1. Endemic goitre
    2. Hyperthyroidism
    3. Myxoedema
    4. Cretinism
(Ref. 5, p. 989)
  1. Normal range of total thyroxine in serum is:
    1. 0.8-2.4 ng/dl
    2. 80-220 ng/dl
    3. 5-12 ng/dl
    4. 5-12 μg/d1
(Ref. 1, p. 870)
  1. Normal range of total tri-iodothyronine in serum is:
    1. 0.1-0.2 ng/dl
    2. 80-220 ng/dl
    3. 0.8-2.4 μg/d1
    4. 5-12μg/d1
(Ref. 1, p. 870)
  1. Administration of TSH increases serum T3 and T4 in:
    1. Hyperthyroidism of pituitary origin
    2. Hyperthyroidism of thyroid origin
    3. Hypothyroidism of pituitary origin
    4. Hypothyroidism of thyroid origin
(Ref. 5, p. 732)
  1. High level of T3 and T4 and low TSH in serum indicates:
    1. Hyperthyroidism of pituitary origin
    2. Hypothyroidism of pituitary origin
    3. Hyperthyroidism of thyroid origin
    4. Hypothyroidism of thyroid origin
(Ref. 5, p. 732)
  1. BMR is increased in:
    1. Endemic goitre
    2. Thyrotoxicosis
    3. Myxoedema
    4. Cretinism
(Ref. 5, p. 993)
  1. Serum cholesterol is decreased in:
    1. Endemic goitre
    2. Thyrotoxicosis
    3. Myxoedema
    4. Cretinism
(Ref. 5, p. 993)
59 B
60 D
61 B
62 C
63 C
64 B
65 B

Metabolism of Xenobiotics27

  1. Cytochrome P-450:
    1. Is a mono-oxygenase
    2. Acts on endogenous substrates
    3. Acts on exogenous substrates
    4. All of the above
(Ref. 1, p. 781)
  1. Cytochrome b5 is required in:
    1. Respiratory chain
    2. Some microsomal hydroxylation reactions
    3. Some mitochondrial hydroxylation reactions
    4. None of the above
(Ref. 1, p.134)
  1. All the following statements about cytochrome P-450 are correct except:
    1. It has 450 isoforms
    2. It is a haemoprotein
    3. It is present in bacteria
    4. It can catalyse a wide range of reactions
(Ref. 1, pp. 780-781)
  1. In addition to hydroxylation reactions, cytochrome P-450 can catalyse:
    1. Dehalogenation
    2. Epoxidation
    3. Reduction
    4. All of the above
(Ref. 1, p. 780)
1 D
2 B
3 A
4 D
317
  1. All the following statements about microsomal hydroxylase system are correct except:
    1. Cytochrome P-450 acts as an enzyme in this system
    2. Some endogenous substrates are hydroxylated by this system
    3. This system makes xenobiotics more soluble
    4. It prevents the conversion of pro-carcinogens into carcinogens
(Ref. 1, pp. 781, 788)
  1. Microsomal and mitochondrial hydroxylase systems have all the following similarities except:
    1. Both require NADPH
    2. Both require iron-sulphur protein
    3. Both contain cytochrome P-450
    4. Both require FAD
(Ref. 1, p. 135)
  1. Microsomal and mitochondrial hydroxylase systems have the following difference:
    1. Microsomal system uses NADPH while the mitochondrial system uses NADH
    2. Microsomal system contains cytochrome P-450 while the mitochondrial system contains cytochrome b5
    3. Microsomal system contains NADPH-cytochrome P-450 reductase while the mitochondrial system contains adrenodoxin reductase
    4. Microsomal system hydroxylates endogenous substrates while the mitochondrial system hydroxylates exogenous substrates
(Ref. 1, p. 781)
  1. Reduced cytochrome P-450 complexed with carbon monoxide:
    1. Absorbs light at 450 nm
    2. Emits light of 450 nm
    3. Becomes more active
    4. None of the above
(Ref. 1, p. 781)
  1. Cytochrome P-450 is present:
    1. Only in liver
    2. Only in liver and adrenal glands
    3. In the highest amount in liver
    4. In the highest amount in adrenal glands
(Ref. 1, p. 781)
5 D
6 B
7 C
8 A
9 C
318
  1. All the following statements about cytochrome P-450 are correct except:
    1. It is found in many species
    2. Several families of cytochrome P-450s exist
    3. Members of one family share at least 55% sequence homology
    4. Cytochrome P-450s have a broad and overlapping substrate specificity
(Ref. 1, p. 781)
  1. All the following statements about cytochrome P-450 are correct except:
    1. Several isoforms of cytochrome P-450 are inducible
    2. Induction by one compound may alter the metabolism of some other compound
    3. Induction may occur by increased transcription, mRNA stabilisation or enzyme stabilisation
    4. Induction of cytochrome P-450 enhances the action of many drugs
(Ref. 1, p. 782)
  1. Prior to excretion, xenobiotics or their metabolites are conjugated most frequently with:
    1. Glucuronic acid
    2. Sulphate
    3. Glutathione
    4. Acetate
(Ref. 1, pp. 782-783)
  1. Glucuronic acid is used to conjugate:
    1. Bilirubin
    2. Steroids
    3. Xenobiotics
    4. All of the above
(Ref. 1, pp. 782-783)
  1. Glutathione is involved in:
    1. Conjugation of some xenobiotics
    2. Detoxification of hydrogen peroxide
    3. Cellular uptake of some amino acids
    4. All of the above
(Ref. 1, p. 783)
  1. Epoxides:
    1. May be formed from some pro-carcinogens
    2. Are highly reactive
    3. Can be converted into less reactive forms by epoxide hydroxylase
    4. All of the above
(Ref. 1, p. 785)
10 C
11 D
12 A
13 D
14 D
15 D

References

 
  1. Murray RK, Granner DK, Mayes PA, Rodwell VW: Harper's Biochemistry, 25th ed. Prentice-Hall International Inc,  2000.
  1. Stryer L: Biochemistry, 3rd ed. WH Freeman and Co,  1995.
  1. Lehninger AL: Principles of Biochemistry, 2nd ed. CBS Publishers and Distributors Pvt Ltd,  Delhi,  1982.
  1. Harper HA, Rodwell VW, Mayes PA: Review of Physiological Chemistry, 16th ed. Lange Medical Publications,  1977.
  1. Chatterjea MN, Shinde R: Textbook of Medical Biochemistry, 2nd ed. Jaypee Brothers Medical Publishers (P) Ltd,  New Delhi,  1995.
  1. Vasudevan DM, Sreekumari S: Textbook of Biochemistry for Medical Students, 2nd ed. Jaypee Brothers Medical Publishers (P) Ltd,  New Delhi,  1998.
  1. Gupta RC, Bhargava S: Practical Biochemistry, 3rd ed. CBS Publishers and Distributors Pvt Ltd,  Delhi,  2004.
Note: Matter pertaining to every question can be found on the page number(s) of the reference cited at the end of the question.