PROTEINS AND PROTEIN METABOLISM MCQS

PROTEINS AND PROTEIN METABOLISM MCQS, Introduction to Biochemistry

1. All proteins contain the

(A) Same 20 amino acids

(B) Different amino acids

(D) Only a few amino acids

2. Proteins contain

(A) Only L- á – amino acids

(B) Only D-amino acids

(D) Both (A) and (B)

3. The optically inactive amino acid is

(A) Glycine (B) Serine

4. At neutral pH, a mixture of amino acids in solution would be predominantly:

(A) Dipolar ions

(B) Nonpolar molecules

(D) Hydrophobic

5. The true statement about solutions of amino acids at physiological pH is

(A) All amino acids contain both positive and

negative charges

(B) All amino acids contain positively charged

side chains

charge

(D) All amino acids contain negatively charged

side chains

6. pH (isoelectric pH) of alanine is

(A) 6.02 (B) 6.6

7. Since the pK values for aspartic acid are 2.0, 3.9 and 10.0, it follows that the isoelectric (pH) is

(A) 3.0 (B) 3.9

8. Sulphur containing amino acid is

(A) Methionine (B) Leucine

9. An example of sulphur containing amino acid is

(A) 2-Amino-3-mercaptopropanoic acid

(B) 2-Amino-3-methylbutanoic acid

(D) Amino acetic acid

10. All the following are sulphur containing amino acids found in proteins except

(A) Cysteine (B) Cystine

11. An aromatic amino acid is

(A) Lysine (B) Tyrosine

12. The functions of plasma albumin are

(A) Osmosis (B) Transport

13. Amino acid with side chain containing

basic groups is

(A) 2-Amino 5-guanidovaleric acid

(B) 2-Pyrrolidine carboxylic acid

(D) 2-Amino propanoic acid

14. An example of á-amino acid not present

in proteins but essential in mammalian

metabolism is

(A) 3-Amino 3-hydroxypropanoic acid

(B) 2-Amino 3-hydroxybutanoic acid

(D) 2-Amino 3-mercaptopropanoic acid

15. An essential amino acid in man is

(A) Aspartate (B) Tyrosine

16. Non essential amino acids

(A) Are not components of tissue proteins

(B) May be synthesized in the body from essential

amino acids

(D) May be synthesized in the body in diseased

states

17. Which one of the following is semiessential

amino acid for humans?

(A) Valine (B) Arginine

18. An example of polar amino acid is

(A) Alanine (B) Leucine

19. The amino acid with a nonpolar side chain

(A) Serine (B) Valine

20. A ketogenic amino acid is

(A) Valine (B) Cysteine

21. An amino acid that does not form an á–

helix is

(A) Valine (B) Proline

22. An amino acid not found in proteins is

(A) â-Alanine (B) Proline

23. In mammalian tissues serine can be a

biosynthetic precursor of

(A) Methionine (B) Glycine

24. A vasodilating compound is produced by

the decarboxylation of the amino acid:

(A) Arginine (B) Aspartic acid

25. Biuret reaction is specific for

(A) –CONH-linkages (B) –CSNH2 group

26. Sakaguchi’s reaction is specific for

(A) Tyrosine (B) Proline

27. Million-Nasse’s reaction is specific for the

amino acid:

(A) Tryptophan (B) Tyrosine

28. Ninhydrin with evolution of CO2 forms a

blue complex with

(A) Peptide bond (B) á -Amino acids

29. The most of the ultraviolet absorption of

proteins above 240 nm is due to their

content of

(A) Tryptophan (B) Aspartate

30. Which of the following is a dipeptide?

(A) Anserine (B) Glutathione

31. Which of the following is a tripeptide?

(A) Anserine (B) Oxytocin

32. A peptide which acts as potent smooth

muscle hypotensive agent is

(A) Glutathione (B) Bradykinin

33. A tripeptide functioning as an important

reducing agent in the tissues is

(A) Bradykinin (B) Kallidin

34. An example of metalloprotein is

(A) Casein (B) Ceruloplasmin

35. Carbonic anhydrase is an example of

(A) Lipoprotein (B) Phosphoprotein

36. An example of chromoprotein is

(A) Hemoglobin (B) Sturine

37. An example of scleroprotein is

(A) Zein (B) Keratin

38. Casein, the milk protein is

(A) Nucleoprotein (B) Chromoprotein

39. An example of phosphoprotein present

in egg yolk is

(A) Ovoalbumin (B) Ovoglobulin

40. A simple protein found in the nucleoproteins

of the sperm is

(A) Prolamine (B) Protamine

41. Histones are

(A) Identical to protamine

(B) Proteins rich in lysine and arginine

(D) Insoluble in water and very dilute acids

42. The protein present in hair is

(A) Keratin (B) Elastin

43. The amino acid from which synthesis of

the protein of hair keratin takes place is

(A) Alanine (B) Methionine

44. In one molecule of albumin the number

of amino acids is

(A) 510 (B) 590

45. Plasma proteins which contain more than

4% hexosamine are

(A) Microglobulins (B) Glycoproteins

46. After releasing O2 at the tissues,

hemoglobin transports

(A) CO2 and protons to the lungs

(B) O2 to the lungs

(D) Nutrients

47. Ehlers-Danlos syndrome characterized by

hypermobile joints and skin abnormalities

is due to

(A) Abnormality in gene for procollagen

(B) Deficiency of lysyl oxidase

(D) Deficiency of lysyl hydroxylase

48. Proteins are soluble in

(A) Anhydrous acetone(B) Aqueous alcohol

49. A cereal protein soluble in 70% alcohol

but insoluble in water or salt solution is

(A) Glutelin (B) Protamine

50. Many globular proteins are stable in

solution inspite they lack in

(A) Disulphide bonds (B) Hydrogen bonds

51. The hydrogen bonds between peptide

linkages of a protein molecules are interfered

(A) Guanidine (B) Uric acid

52. Globular proteins have completely folded,

coiled polypeptide chain and the axial

ratio (ratio of length to breadth) is

(A) Less than 10 and generally not greater than

3–4

(B) Generally 10

(D) Greater than 10

53. Fibrous proteins have axial ratio

(A) Less than 10

(B) Less than 10 and generally not greater than

3–4

(D) Greater than 10

54. Each turn of α-helix contains the amino

acid residues (number):

(A) 3.6 (B) 3.0

55. Distance traveled per turn of á−helix in

nm is

(A) 0.53 (B) 0.54

56. Along the á-helix each amino acid residue

advances in nm by

(A) 0.15 (B) 0.10

57. The number of helices present in a

collagen molecule is

(A) 1 (B) 2

58. In proteins the á-helix and â-pleated sheet

are examples of

(A) Primary structure (B) Secondary structure

59. The a-helix of proteins is

(A) A pleated structure

(B) Made periodic by disulphide bridges

(D) Stabilised by hydrogen bonds between NH

and CO groups of the main chain

60. At the lowest energy level á-helix of

polypeptide chain is stabilised

(A) By hydrogen bonds formed between the H of

peptide N and the carbonyl O of the residue

(B) Disulphide bonds

(D) Ester bonds

61. Both á-helix and â-pleated sheet conformation

of proteins were proposed by

(A) Watson and Crick

(B) Pauling and Corey

(D) Y.S.Rao

62. The primary structure of fibroin, the

principal protein of silk worm fibres

consists almost entirely of

(A) Glycine (B) Aspartate

63. Tertiary structure of a protein describes

(A) The order of amino acids

(B) Location of disulphide bonds

(D) The ways of protein folding

64. In a protein molecule the disulphide bond

is not broken by

(A) Reduction

(B) Oxidation

(D) X-ray diffraction

65. The technique for purification of proteins

that can be made specific for a given

protein is

(A) Gel filtration chromotography

(B) Ion exchange chromatography

(D) Affinity chromatography

66. Denaturation of proteins results in

(A) Disruption of primary structure

(B) Breakdown of peptide bonds

(D) Irreversible changes in the molecule

67. Ceruloplasmin is

(A) á1-globulin (B) á2-globulin

68. The lipoprotein with the fastest electrophoretic

mobility and the lowest triglyceride

content is

(A) Chylomicron (B) VLDL

69. The lipoprotein associated with activation

of LCAT is

(A) HDL (B) LDL

70. The apolipoprotein which acts as activator

of LCAT is

(A) A-I (B) A-IV

71. The apolipoprotein which acts as actiator

of extrahepatic lipoprotein is

(A) Apo-A (B) Apo-B

72. The apolipoprotein which forms the

integral component of chylomicron is

(A) B-100 (B) B-48

73. The apolipoprotein which from the

integral component of VLDL is

(A) B-100 (B) B-48

74. The apolipoprotein which acts as ligand

for LDL receptor is

(A) B-48 (B) B-100

75. Serum LDL has been found to be increased

(A) Obstructive jaundice

(B) Hepatic jaundice

(D) Malabsorption syndrome

76. A lipoprotein associated with high

incidence of coronary atherosclerosis is

(A) LDL (B) VLDL

77. A lipoprotein inversely related to the

incidence of coronary artherosclerosis is

(A) VLDL (B) IDL

78. The primary biochemical lesion in homozygote

with familial hypercholesterolemia

(type IIa) is

(A) Loss of feed back inhibition of HMG

reductase

(B) Loss of apolipoprotein B

(D) Functional deficiency of plasma membrane

receptors for LDL

79. In abetalipoproteinemia, the biochemical

defect is in

(A) Apo-B synthesis

(B) Lipprotein lipase activity

(D) LCAT activity

80. Familial hypertriaacylglycerolemia is

associated with

(A) Over production of VLDL

(B) Increased LDL concentration

(D) Slow clearance of chylomicrons

81. For synthesis of prostaglandins, the

essential fatty acids give rise to a fatty

acid containing

(A) 12 carbon atoms (B) 16 carbon atoms

82. All active prostaglandins have at least one

double bond between positions

(A) 7 and 8 (B) 10 and 11

83. Normal range of plasma total phospholipids

(A) 0.2–0.6 mmol/L (B) 0.9–2.0 mmol/L

84. HDL2 have the density in the range of

(A) 1.006–1.019 (B) 1.019–1.032

85. â-lipoproteins have the density in the

range of

(A) 0.95–1.006 (B) 1.006–1.019

86. IDL have the density in the range of

(A) 0.95–1.006 (B) 1.006–1.019

87. Aspirin inhibits the activity of the enzyme:

(A) Lipoxygenase (B) Cyclooxygenase

88. A ’suicide enzyme’ is

(A) Cycloxygenase (B) Lipooxygenase

89. In adipose tissue prostaglandins

decrease

(A) Lipogenesis (B) Lipolysis

90 The optimal pH for the enzyme pepsin is

(A) 1.0–2.0 (B) 4.0–5.0

91. Pepsinogen is converted to active pepsin

(A) HCl (B) Bile salts

92. The optimal pH for the enzyme rennin is

(A) 2.0 (B) 4.0

93. The optimal pH for the enzyme trypsin is

(A) 1.0–2.0 (B) 2.0–4.0

94. The optimal pH for the enzyme chymotrypsin

(A) 2.0 (B) 4.0

95 Trypsinogen is converted to active trypsin

(A) Enterokinase (B) Bile salts

96 Pepsin acts on denatured proteins to

produce

(A) Proteoses and peptones

(B) Polypeptides

(D) Dipeptides

97. Renin converts casein to paracasein in

presence of

(A) Ca++ (B) Mg++

98. An expopeptidase is

(A) Trypsin (B) Chymotrypsin

99. The enzyme trypsin is specific for peptide

bonds of

(A) Basic amino acids

(B) Acidic amino acids

(D) Next to small amino acid residues

100. Chymotrypsin is specific for peptide bonds

containing

(A) Uncharged amino acid residues

(B) Acidic amino acids

(D) Small amino acid residues

101. The end product of protein digestion in

G.I.T. is

(A) Dipeptide (B) Tripeptide

102. Natural L-isomers of amino acids are

absorbed from intestine by

(A) Passive diffusion (B) Simple diffusion

103. Abnormalities of blood clotting are

(A) Haemophilia (B) Christmas disease

104. An important reaction for the synthesis

of amino acid from carbohydrate

intermediates is transamination which

requires the cofactor:

(A) Thiamin (B) Riboflavin

105. The main sites for oxidative deamination

are

(A) Liver and kidney

(B) Skin and pancreas

(D) Lung and spleen

106. A positive nitrogen balance occurs

(A) In growing infant

(B) Following surgery

(D) In kwashiorkar

107. The main site of urea synthesis in mammals

(A) Liver (B) Skin

108. The enzymes of urea synthesis are found

(A) Mitochondria only

(B) Cytosol only

(D) Nucleus

109. The number of ATP required for urea

synthesis is

(A) 0 (B) 1

110. Most of the ammonia released from L-á–

amino acids reflects the coupled action of

transaminase and

(A) L-glutamate dehydrogenase

(B) L-amino acid oxidase

(D) Serine dehydratase

111. In urea synthesis, the amino acid functioning

solely as an enzyme activator:

(A) N-acetyl glutamate (B) Ornithine

112. The enzyme carbamoyl phosphate

synthetase requires

(A) Mg++ (B) Ca++

113. Control of urea cycle involves the enzyme:

(A) Carbamoyl phosphate synthetase

(B) Ornithine transcarbamoylase

(D) Arginase

114. Transfer of the carbamoyl moiety of

carbamoyl phosphate to ornithine is

catalysed by a liver mitochondrial enzyme:

(A) Carbamoyl phosphate synthetase

(B) Ornithine transcarbamoylase

(D) N-acetyl glutamate hydrolase

115. A compound serving a link between citric

acid cycle and urea cycle is

(A) Malate (B) Citrate

116. The 2 nitrogen atoms in urea are

contributed by

(A) Ammonia and glutamate

(B) Glutamine and glutamate

(D) Ammonia and alanine

117. In carcinoid syndrome the argentaffin

tissue of the abdominal cavity overproduce

(A) Serotonin (B) Histamine

118. Tryptophan could be considered as

precursor of

(A) Melanotonin (B) Thyroid hormones

119. Conversion of tyrosine to dihydroxyphenylalanine

is catalysed by tyrosine hydroxylase

which requires

(A) NAD (B) FAD

120. The rate limiting step in the biosynthesis

of catecholamines is

(A) Decarboxylation of dihydroxyphenylalanine

(B) Hydroxylation of phenylalanine

(D) Oxidation of dopamine

121. The enzyme dopamine â-oxidase which

catalyses conversion of dopamine to

norepinephrine requires

(A) Vitamin A (B) Vitamin C

122. In humans the sulphur of methionine and

cysteine is excreted mainly as

(A) Ethereal sulphate

(B) Inorganic sulphate

(D) Thioorganic compound

123. Small amount of urinary oxalates is

contributed by the amino acid:

(A) Glycine (B) Tyrosine

124. The amino acid which detoxicated benzoic

acid to form hippuric acid is

(A) Glycine (B) Alanine

125. The amino acids involved in the synthesis

of creatin are

(A) Arginine, glycine, active methionine

(B) Arginine, alanine, glycine

(D) Arginine, lysine, methionine

126. Chemical score of egg proteins is considered

to be

(A) 100 (B) 60

127. Chemical score of milk proteins is

(A) 70 (B) 65

128. Chemical score of proteins of bengal gram

(A) 70 (B) 60

129. Chemical score of protein gelatin is

(A) 0 (B) 44

130 Chemical score of protein zein is

(A) 0 (B) 57

131. Biological value of egg white protein is

(A) 94 (B) 83

132. Net protein utilisation of egg protein is

(A) 75% (B) 80%

133. Net protein utilization of milk protein is

(A) 75% (B) 80%

134. A limiting amino acid is an essential

amino acid

(A) That is most deficient in proteins

(B) That is most excess in proteins

(D) That which increases the weight gain

135. The limiting amino acid of rice is

(A) Lysine (B) Tryptophan

136. The limiting amino acid of fish proteins is

(A) Tryptophan (B) Cysteine

137. Pulses are deficient in

(A) Lysine (B) Threonine

138. A trace element deficient in the milk is

(A) Magnesium (B) Copper

139. A conjugated protein present in the egg

yolk is

(A) Vitellin (B) Livetin

140. The chief protein of cow’s milk is

(A) Albumin (B) Vitellin

141. A water soluble vitamin deficient in egg is

(A) Thiamin (B) Ribofalvin

142. Pulses are rich in

(A) Lysine (B) Methionine

143. Milk is deficient in

(A) Vitamin B1 (B) Vitamin B2

144. Milk is deficient in

(A) Calcium (B) Iron

145. When net protein utilization (NPU) is low,

the requirements for proteins are

(A) High (B) Moderate

146. Protein content of human milk is about

(A) 1.4% (B) 2.4%

147. Protein content of cow’s milk is about

(A) 2.5% (B) 3.5%

148. Protein content of soyabean is about

(A) 30% (B) 40%

149. Lipid content of egg white is

(A) 12% (B) 33%

150. The recommended daily allowance (RDA)

of proteins for an adult man is

(A) 70 gms (B) 50 gms

151. The basic amino acids are

(A) Lysine (B) Bile acids

152. The daily caloric requirement for the

normal adult female is about

(A) 1500 (B) 2100

153. In the total proteins, the percentage of

albumin is about

(A) 20–40 (B) 30–45

154. In the total proteins percentage of α1

globulin is about

(A) 0.2–1.2% (B) 1.2–2.0%

155. In the total proteins the percentage of

γ globulin is about

(A) 2.4–4.4% (B) 10.0–21.0%

156. Most frequently the normal albumin

globulin ratioratio (A : G) is

(A) 1.0 : 0.8 (B) 1.5 : 1.0

157. In Thymol turbidity test the protein

involved is mainly

(A) Albumin (B) á1-Globulin

158. In quaternary structure, subunits are

linked by

(A) Peptide bonds (B) Disulphide bonds

159. Molecular weight of human albumin is

about

(A) 156,000 (B) 90,000

160. At isoelectric pH, an amino acid exists as

(A) Anion (B) Cation

161. A disulphide bond can be formed

between

(A) Two methionine residues

(B) Two cysteine residues

(D) All of these

162 A coagulated protein is

(A) Insoluble

(B) Biologically non-functional

(D) All of the above

163. At a pH below the isoelectric point, an

amino acid exists as

(A) Cation

(B) Anion

(D) Undissociated molecule

164. An amino acid having a hydrophilic side

chain is

(A) Alanine (B) Proline

165. An amino acid that does not take part in

á helix formation is

(A) Histidine (B) Tyrosine

166. A protein rich in cysteine is

(A) Collagen (B) Keratin

167. Primary structure of proteins can be

determined by the use of

(A) Electrophoresis (B) Chromatography

168. Electrostatic bonds can be formed between

the side chains of

(A) Alanine and leucine

(B) Leucine and valine

(D) Lysine and aspartate

169. Sanger’s reagent contains

(A) Phenylisothiocyanate

(B) Dansyl chloride

(D) Ninhydrin

170. The most abundant protein in mammals is

(A) Albumin (B) Haemoglobin

171. Folding of newly synthesized proteins is

accelerated by

(A) Protein disulphide isomerase

(B) Prolyl cis-trans isomerase

(D) All of these

172. Primary structure of a protein is formed by

(A) Hydrogen bonds (B) Peptide bonds

173. á-Helix is formed by

(A) Hydrogen bonds

(B) Hydrophobic bonds

(D) Disulphide bonds

174. Glutelins are present in

(A) Milk (B) Eggs

175. Aromatic amino acids can be detected by

(A) Sakaguchi reaction

(B) Millon-Nasse reaction

(D) Xanthoproteic reaction

176. Two amino groups are present in

(A) Leucine (B) Glutamate

177. During denaturation of proteins, all of the

following are disrupted except

(A) Primary structure (B) Secondary structure

178. All the following are branched chain

amino acids except

(A) Isoleucine (B) Alanine

179. An –OH group is present in the side chain of

(A) Serine (B) Arginine

180. Edman’s reagent contains

(A) Phenylisothiocyanate

(B) 1-Fluoro-2, 4-dinitrobenzene

(D) tBOC azide

181. Edman’s reaction can be used to

(A) Determine the number of tyrosine residues in

a protein

(B) Determine the number of aromatic amino acid

residues in a protein

protein

(D) Hydrolyse the peptide bonds in a protein

182. Inherited deficiency of â−glucosidase causes

(A) Tay-Sachs disease

(B) Metachromatic leukodystrophy

(D) Multiple sclerosis

183. Tay-Sachs disease results from inherited

deficiency of

(A) Arylsulphatase A

(B) Hexosaminidase A

(D) Ceramidase

184. The largest alpolipoprotein is

(A) Apo E (B) Apo B-48

185. Apolipoprotein B-100 is synthesised in

(A) Adipose tissue (B) Liver

186. Apolipoprotein B-48 is synthesized in

(A) Adipose tissue (B) Liver

187. Apolipoproteins A-I and A-II are present

(A) LDL only

(B) LDL and VLDL

(D) HDL and chylomicrons

188. Apolipoprotein B-48 is present in

(A) Chylomicrons (B) VLDL

189. Apolipoprotein B-100 is present in

(A) Chylomicrons (B) VLDL only

190. Apolipoproteins C-I, C-II and C-III are

present in

(A) Chylomicrons (B) VLDL

191. Apolipoprotiens C-I, C-II and C-III are

present in all of the following except

(A) Chylomicrons (B) VLDL

192. Apolipoprotein A-I acts as

(A) Enzyme activator (B) Ligand for receptor

193. Apolipoprotien B-100 acts as

(A) Enzyme activator (B) Ligand for receptor

194. Apolipoprotein C-II is an activator of

(A) Lecithin cholesterola acyl transferase

(B) Phospholipase C

(D) Hepatic lipoprotein lipase

195. Nascent chylomicron receives apolipoproteins

C and E from

(A) VLDL remnant (B) VLDL

196. Terminal transferase

(A) Removes nucleotides from 3’ end

(B) Adds nucleotides at 3’ end

(D) Adds nucleotides at 3’end

197. S1 nuclease hydrolyses

(A) DNA of somatic cells

(B) DNA of sperms

(D) Any single stranded DNA

198. Positive nitrogen balance is seen in

(A) Starvation

(B) Wasting diseases

(D) Intestinal malabsorption

199. Alanine can be synthesized from

(A) Glutamate and á-ketoglutarate

(B) Pyruvate and glutamate

(D) Asparate and á-ketoglutarate

200. All of the following are required for

synthesis of alanine except

(A) Pyruvate (B) á-ketoglutarate

201. All of the following statements about

aspartate are true except

(A) It is non-essential amino acid

(B) It is a dicarboxylic amino acid

glutamate

(D) It can be converted into asparagine

202. Glycine can be synthesized from

(A) Serine (B) Choline

203. All of the following are required for

synthesis of glutamine except

(A) Glutamate

(B) Ammonia

(D) ATP

204. A coenzyme required for the synthesis of

glycine from serine is

(A) ATP

(B) Pyridoxal phosphate

(D) NAD

205. All of the following statements about

proline are true except

(A) It is an imino acid

(B) It can be synthesized from glutamate

(D) Free proline can be hydroxylated to

hydroxyproline

206. A protein rich in hydroxyproline is

(A) Prolamin (B) Procollagen

207. All the following statement about

hydroxyproline are true except

(A) There is no codon for hydroxyproline

(B) It is present in large amounts in collagen

hydroxyproline

(D) Hydroxylation of proline residues is catalysed

by a dioxygenase

208. All of the following are required for

hydroxylation of proline residues except

(A) Ascorbic acid (B) Glutamate

209. Cysteine can be synthesized from

methionine and

(A) Serine (B) Homoserine

210. Methionine is synthesized in human body

from

(A) Cysteine and homoserine

(B) Homocysteine and serine

(D) None of these

211. Hydroxylation of phenylalanine requires

all of the following except

(A) Phenylalanine hydroxylase

(B) Tetrahydrobiopterin

(D) Molecular oxygen

212. Non-Protein amino acids are

(A) Ornithine

(B) â-alanine

(D) All of these

213. The amino acid that undergoes oxidative

deamination at significant rate is

(A) Alanine (B) Aspartate

214. Allosteric inhibitor of glutamate dehydrogenase

(A) ATP (B) ADP

215. Allsoteric activator of glutamate dehydrogenase

(A) ATP (B) GTP

216. Free ammonia is released during

(A) Oxidative deamination of glutamate

(B) Catabolism of purines

(D) All of these

217. An organ which is extremely sensitive to

ammonia toxicity is

(A) Liver (B) Brain

218. Ammonia is transported from muscles to

liver mainly in the form of

(A) Free ammonia (B) Glutamine

219. The major site of urea synthesis is

(A) Brain (B) Kidneys

220. Carbamoyl phosphate required for urea

synthesis is formed in

(A) Cytosol (B) Mitochondria

221. Cytosolic and mitochondrial carbamoyl

phosphate synthetase have the following

similarity:

(A) Both use ammonia as a substance

(B) Both provide carbamoyl phosphate for urea

synthesis

activator

(D) Both are allosteric enzymes

222. The following enzyme of urea cycle is

present in cytosol:

(A) Argininosuccinic acid synthetase

(B) Argininosuccinase

(D) All of these

223. ATP is required in following reactions of

urea cycle:

(A) Synthesis of carbamoyl phosphate and

citrulline

(B) Synthesis of citrulline and argininosuccinate

(D) Synthesis of carbamoyl phosphate and

argininosuccinate

224. Daily excretion of nitrogen by an adult

man is about

(A) 15–20 mg (B) 1.5–2 gm

225. Maple syrup urine diseases is an inborn

error of metabolism of

(A) Sulphur-containing amino acids

(B) Aromatic amino acids

(D) Dicarboxylic amino acids

226. Cystinuria results from inability to

(A) Metabolise cysteine

(B) Convert cystine into cysteine

(D) Reabsorb cystine in renal tubules

227. The defective enzyme in histidinemia is

(A) Histidine carboxylase

(B) Histidine decarboxylase

(D) Histidine oxidase

228. All the following statements about

phenylketonuria are correct except

(A) Phenylalanine cannot be converted into

tyrosine

(B) Urinary excretion of phenylpyruvate and

phenyllactate is increased

diet

(D) It leads to decreased synthesis of thyroid

hormones, catecholamines and melanin

229. All the following statements about

albinism are correct except

(A) Tyrosine hydroxylase (tyrosinase) is absent or

deficient in melanocytes

(B) Skin is hypopigmented

(D) Eyes are hypopigmented

230. Glycine is not required for the formation

(A) Taurocholic acid (B) Creatine

231. Histamine is formed from histidine by

(A) Deamination (B) Dehydrogenation

232. DOPA is an intermediate in the synthesis

(A) Thyroid hormones

(B) Catecholamines

(D) Catecholamines and melanin

233. All the following statements about pepsin

are correct except

(A) It is smaller than pepsinogen

(B) It is formed by the action of HCl on its precursor

(D) It hydrolyses the C-terminal and N-terminal

peptide bonds of proteins

234. Pancreatic juice contains the precursors of

all of the following except

(A) Trypsin (B) Chymotrypsin

235. The only correct statement about chymotrypsin

(A) It is formed from trypsin

(B) Carboxypeptidase converts trypsin into

chymotrypsin

(D) It hydrolyses peptide bonds involving basic

amino acids

236. The portion of the antigen molecule which

is recognized by antibody is known as

(A) Hapten (B) Epitope

237. All the following statements about

haptens are true except

(A) They have high molecular weights

(B) They cannot elicit an immune response by

themselves

molecule, they can elicit an immune response

(D) Once an immune response develops, the free

hapten can be recognized by the antibody

238. Antigens and haptens have the following

similarity:

(A) They have high molecular weights

(B) They can elicit immune response by themselves

association with some other large molecule

(D) Once an immune response develops, free

antigen and free hapten can be recognized

by the antibody

239. The minimum number of polypeptide

chains in an immunoglobulin is

(A) Two (B) Four

240. Light chains of immunoglobulins are of

following types:

(A) Alpha and kappa (B) Alpha and gamma

241 Immunoglobulins are classified on the

basis of

(A) Type of light chains

(B) Type of heavy chains

(D) Molecular weight

242. The molecular weight of light chains is

(A) 10,000–15,000 (B) 20,000–25,000

243. The molecular weight of heavy chains is

(A) 20,000–25,000 (B) 25,000–50,000

244. Secretory component is present in

(A) IgA (B) IgG

245. The variable region of light chains is the

(A) N-terminal quarter (B) N-terminal half

246. The variable region of light chain is the

(A) N-terminal quarter

(B) N-terminal half

(D) C-terminal half

247. The variable region of light chains has

(A) One hypervariable region

(B) Two hypervariable regions

(D) Four hypervariable regions

248. The variable region of heavy chains has

(A) One hypervariable region

(B) Two hypervariable regions

(D) Four hypervariable regions

249. The most abundant immunoglobulin in

plasma is

(A) IgA (B) IgG

250. The largest immunoglobulin is

(A) IgA (B) IgG

251. The plasma concentration of IgA is

(A) 1–5 mg/dl (B) 40–200 mg/dl

252. An immunoglobulin found in exocrine

secretions is

(A) IgA (B) IgG

253. Allergic reactions are mediated by

(A) IgA (B) IgG

254. An immunoglobulin which can cross the

placental barrier is

(A) IgA (B) IgM

255. IgM possesses

(A) Two light chains and two heavy chains

(B) Four light chains and four heavy chains

(D) Ten light chains and ten heavy chains

256. The immunoglobulin having the longest

half-life is

(A) IgA (B) IgG

257. The half-life of IgG is

(A) 2–3 days (B) 5–6 days

258. Recognition of antigen is the function of

(A) Variable region of light chains

(B) Variable regions of light and heavy chains

(D) Constant regions of light and heavy chains

259. The effector function of antibody is

performed by

(A) Variable region of light chains

(B) Constant region of heavy chains

(D) Constant regions of light and heavy chains

260. Complement system can be activated by

binding of antigen to

(A) IgA (B) IgD

261. C1 component of classical complement

pathway is made up of

(A) Complements 1q and 1r

(B) Complements 1q and 1s

(D) Complements 1q, 1r and 1s

262. The components of complement system

are activated by

(A) Microsomal hydroxylation

(B) Phosphorylation

(D) Proteloysis

263. The component system forms a membrane

attack complex made up of

(A) Complements 1q, 1r and 1s

(B) Complements 1, 2, 3 and 4

(D) Factors B and D

264. Factors B and D are required in

(A) The classical pathway of complement fixation

(B) The alternate complement pathway

(D) None of these

265. The alternate complement pathway

doesn’t involve

(A) Antigen-antibody complex

(B) Complement 3

(D) Membrane attack unit

266. Antibody diversity arises from

(A) Gene amplification

(B) Gene re-arrangement

(D) All of these

267. A light chain gene is constructed from the

following segments:

(A) Variable and constant segments

(B) Variable, joining and constant segments

(D) Variable, joining, diversity and constant

segments

268. In metabolic point of view, amino acids

are classified as

(A) Glycogenic

(B) Ketogenic

(D) All of these

269. Diversity segments are present in

(A) Light chain genes

(B) Heavy chain genes

(D) None of these

270. Constant segments of heavy chains are

(A) Five types (B) Six types

271. Gamma heavy chains are of

(A) Two types (B) Three types

272. Gamma heavy chains are present in

(A) IgA (B) IgG

273. Heavy chains in IgD are of following type:

(A) Alpha (B) Gamma

274. On exposure to any antigen, the first

antibody to be formed is of the following

class:

(A) IgA (B) IgG

275. Constant segment genes of heavy chains

are present in a cluster in which the first

gene on side is

(A) Alpha (B) Gamma

276. Cell-mediated immunity is the function of

(A) B lymphocytes (B) T lymphocytes

277. The most abundant T cells are

(A) Cytotoxic T cells (B) Helper T cells

278. T cells can recognise

(A) Free antigens

(B) Antigens bound to cells

(D) Antigens bound to MHC proteins

279. MHC proteins are unique to

(A) Each cell (B) Each organ

280. MHC class I proteins are present on the

surface of

(A) B cells only (B) T cells only

281. MHC class I proteins, in conjunction with

antigens are recognised by

(A) Cytotoxic T cells (B) Helper T cells

282. MHC class II proteins are present on the

surface of

(A) All cells

(B) B lymphocytes only

(D) Macrophages and B lymphocytes

283. MHC Class II proteins, in conjunction with

antigens, are recognised by

(A) Cytotoxic T cells

(B) Helper T cells

(D) Memory T cells

284. CD 8 is a transmembrane glycoprotein

present in

(A) Cytotoxic T cells

(B) Helper T cells

(D) Memory T cells

285. CD 4 is a transmembrane glycoprotein

present in

(A) Cytotoxic T cells (B) Helper T cells

286. CD 3 complex and p 56lck proteins are

present in

(A) Cytotoxic T cells (B) Helper T cells

287. Cytotoxic T cells release

(A) Perforins

(B) Interleukins

(D) Tumour necrosis factor

288. Helper T cells release

(A) Interleukins

(B) Colony stimulating factors

(D) All of these

289. MHC Class III proteins include

(A) Immunoglobulins

(B) Components of complement system

(D) CD4 and CD8 proteins

290. Human immunodeficiency virus destroys

(A) Cytotoxic T cells (B) Helper T cells

291. In allergic diseases, the concentration of

the following is increased in plasma:

(A) IgA (B) IgG

292. IgE has a tendency to attach to

(A) Basophils (B) Mast cells

293. Reaginic antibody is

(A) IgA (B) IgG

294. Active immunity can be produced by

administration of

(A) Killed bacteria or viruses

(B) Live attenuated bacteria or viruses

(D) All of these

295. Passive immunity can be produced by

administration of

(A) Pure antigens

(B) Immunoglobulins

(D) Killed bacteria or viruses

296. Helper T cells release all the following

except

(A) Interleukins

(B) Colony stimulating factors

(D) Tumour necrosis factor

297. IgG cleaved by papain into

(A) Two light and two heavy chains

(B) Two Fab and one Fc fragments

each

(D) One Fab and two Fc fragments

298. Bence-Jones protein is

(A) An immunoglobulin

(B) A dimer of heavy chains

(D) A dimer of one heavy and one light chains

299. Bence-Jones proteins possess all the

following properties except

(A) They are dimers of light chains

(B) Their amino acids sequences are identical

acid sequences

(D) Their C-terminal halves have constant amino

acid sequences

300. A Zwitterion is

(A) Positive ion (B) Negative ion

301. After accounting for SDA, the net gain of

energy from 25 gm of proteins is about

(A) 70 kcal (B) 100 kcal

302. After accounting for SDA, the net gain of

energy from 25 gm of carbohydrates is

about

(A) 70 kcal (B) 95 kcal

303. After accounting for SDA, the net gain of

energy from 100 gm of fat is about

(A) 600 kcal (B) 780 kcal

304. If proteins, carbohydrates and fats are

consumed together:

(A) The total SDA is the sum of individual SDAs

of proteins, carbohydrates and fats

(B) The total SDA is more than the sum of

individual SDAs of proteins, carbohydrates

and fats

proteins

(D) Proteins raise the SDA of carbohydrates and

fats

305. After calculating the energy requirement

of a person:

(A) 10% kcal are subtracted on account of SDA

(B) 10% kcal are added on account of SDA

(D) 20% kcal are subtracted on account of SDA

306. The recommended energy intake for an

adult sedentary Indian man is

(A) 1,900 kcal/day (B) 2,400 kcal/day

307. The recommended energy intake for an

adult sedentary Indian woman is

(A) 1,900 kcal/day (B) 2,200 kcal/day

308. During pregnancy, the following should

be added to the calculated energy

requirement:

(A) 300 kcal/day (B) 500 kcal/day

309. During first six months of lactation, the

following increment in energy intake is

recommended:

(A) 200 kcal/day (B) 300 kcal/day

310. The proximate principles of diet are

(A) Vitamins and minerals

(B) Proteins

(D) Carbohydrates, fats and proteins

311. The limiting amino acid in wheat is

(A) Leucine (B) Lysine

312. The limiting amino acid in pulses is

(A) Leucine (B) Lysine

313. Maize is poor in

(A) Lysine

(B) Methionine

(D) Lysine and tryptophan

314. The percentage of ingested protein/

nitrogen absorbed into blood stream is

known as

(A) Net protein utilisation

(B) Protein efficiency ratio

(D) Biological value of protein

315. Biological value of a protein is

(A) The percentage of ingested protein/nitrogen

absorbed into circulation

(B) The percentage of ingested protein/nitrogen

in the body

for protein synthesis in the body

(D) The gain in body weight (gm) per gm of

protein ingested

316. Net protein utilisation depends upon

(A) Protein efficiency ratio

(B) Digestibility coefficient

ratio

(D) Digestibility coefficient and biological value

317. The gain in body weight (gm) per gm of

protein ingested is known as

(A) Net protein utilisation

(B) Protein efficiency ratio

(D) Biological value of protein

318. The following is considered as reference

standard for comparing the nutritional

quality of proteins:

(A) Milk proteins (B) Egg proteins

319. Biological value of egg proteins is about

(A) 70 % (B) 80 %

320. The following has the highest protein

efficiency ratio:

(A) Milk proteins (B) Egg proteins

321. The following has the lowest protein

efficiency ratio:

(A) Maize proteins (B) Wheat proteins

322. Protein content of egg is about

(A) 10% (B) 13%

323. Protein content of meat is about

(A) 10% (B) 13%

324. Protein content of rice is about

(A) 7% (B) 12%

325. The calorific value of wheat is about

(A) 2.5 kcal/gm (B) 3.5 kcal/gm

326. For vegetarians, pulses are an important

source of

(A) Carbohydrates (B) Proteins

327. The amino acids present in pulses can

supplement the limiting amino acids of

(A) Cereals (B) Milk

328. Milk is a good source of

(A) Proteins, calcium and iron

(B) Proteins, calcium and ascorbic acid

(D) Proteins, lactose and essential fatty acids

329. Milk is a good source of all of the following

except

(A) Essential amino acids

(B) Vitamin C

(D) Calcium and phosphorous

330. Milk is poor in

(A) Cholesterol (B) Retinol

331. Egg is rich in all of the following except

(A) Cholesterol (B) Saturated fatty acids

332. A phosphoprotein present in egg is

(A) Casein (B) Albumin

333. Consumption of raw eggs can cause

deficiency of

(A) Calcium (B) Lipoic acid

334. Egg is poor in

(A) Essential amino acids

(B) Carbohydrates

(D) Biotin

335. Cholesterol is present in all the following

except

(A) Milk (B) Fish

336. Meat is rich in all of the following except

(A) Iron (B) Fluorine

337. Kwashiorkor occurs when the diet is

severely deficient in

(A) Iron (B) Calories

338. Clinical features of Kwashiorkor include

all of the following except

(A) Mental retardation (B) Muscle wasting

339. Kwashiorkor usually occurs in

(A) The post-weaning period

(B) Pregnancy

(D) Old age

340. Marasmus occurs from deficient intake of

(A) Essential amino acids

(B) Essential fatty acids

(D) Zinc

341. Marasmus differs from Kwashiorkor in

the which of these following respect

(A) Mental retardation occurs in kwashiorkor but

not in marasmus

(B) Growth is retarded in kwashiorkor but not in

marasmus

kwashiorkor

(D) Subcutaneous fat disappears in marasmus

but not in kwashiorkor

342. Energy reserves of an average well-fed

adult man are about

(A) 50,000 kcal (B) 100,000 kcal

343. During starvation, the first reserve

nutrient to be depleted is

(A) Glycogen (B) Proteins

344. Synthesis of the following enzymes is

increased during starvation.

(A) Digestive enzymes

(B) Gluconeogenic enzymes

(D) Glucokinase

345. In hypoparathyroidism

(A) Plasma calcium and inorganic phosphorous

are low

(B) Plasma calcium and inorganic phosphorous

are high

phosphorous high

(D) Plasma calcium is high and inorganic

phosphorous low

346. The number of amino acid residues in

calcitonin in

(A) 9 (B) 32

347. Calcitonin is synthesised in

(A) Parathyroid glands

(B) Thyroid gland

(D) Adrenal cortex

348. Plasma calcium is lowered by

(A) Parathormone (B) Calcitonin

349. á Cells of Islets of Langerhans secrete

(A) Insulin (B) Glucagon

350. A/G ratio is

(A) Strength of proteins

(B) ratio of serum proteins

(D) None of these

351. Insulin is made up of

(A) A single polypeptide chain having 51 amino

acid residues

(B) A single polypeptide chain having 84 amino

acid residues

amino acid residues

(D) A-chain having 30 and B-chain having 21

amino acid residues

352. The number of amino acid residues in preproinsulin

(A) 51 (B) 84

353. Pre-proinsulin contains a signal sequence

having

(A) 9 amino acid residues

(B) 19 amino acid residues

(D) 33 amino acid residues

354. The number of intra-chain disulphide

bonds in pro-insulin:

(A) One (B) Two

355. Pentagastrin is a

(A) Naturally occurring form of gastrin

(B) Inactive metabolite of gastrin

(D) Synthetic form of gastrin

356. Secretion of gastrin is evoked by

(A) Entry of food into stomach

(B) Vagal stimulation

(D) All of these

357. Gastrin stimulates

(A) Gastric motility (B) Gastric secretion

358. Secretin is made up of

(A) 17 amino acids (B) 27 amino acids

359. Secretin causes all of the following except

(A) Secretion of pancreatic juice

(B) Secretion of bile

(D) Stimulation of intestinal motility

360. All of the following statements about

cholecystokinin pancreozymin are true

except

(A) It is secreted by mucosa of small intestine

(B) It stimulates secretion of pancreatic juice rich

in enzymes

(D) It inhibits gastric motility

361. All of the following statements about

pancreatic somatostain are true except

(A) It is secreted by ä cells of islets of Langerhans

(B) It stimulates the secretion of gastrin

(D) It inhibits the secretion of cholecystokininpancreozymin

362. Histidine is converted into histamine by

(A) Carboxylation (B) Decarboxylation

363. Histamine is synthesised in

(A) Brain (B) Mast cells

364. Histamine causes all the following except

(A) Stimulation of gastric secretion

(B) Vasoconstriction

(D) Increase in capillary permeability

365. H2-receptors are blocked by

(A) Diphenhydramine (B) Mepayramine

366. Serotonin is synthesised from

(A) Serine (B) Phenylalanine

367. All the following statements about

serotonin are true except

(A) It causes vasolidatation

(B) It causes bronchoconstriction

(D) Its metabolite is 5-hydroxyindole acetic acid

368. All the following statements about

angiotensin are true except

(A) Its precursor is an á2-globulin

(B) Its active form is an octapeptide

(D) It increases the secretion of aldosterone

369. Methyl dopa decreases blood pressure by

(A) Inhibiting the synthesis of catecholamines

(B) Antagonising the action of aldosterone

(D) Inhibiting the breakdown of angiotensin

370. Binding of gamma-aminobutyric acid to

its receptors in brain increases the

permeability of cell membrane to

(A) Cl– (B) Na+

371. Binding of acetylcholine to its receptors

increases the permeability of cell

membrane to

(A) Ca++ (B) Na+

372. All of the following are glycoproteins

except

(A) Collagen (B) Albumin

373. Sialic acids are present in

(A) Proteoglycans (B) Glycoproteins

374. Hyaluronidase hydrolyses

(A) Hyaluronic acid

(B) Chondroitin sulphate

(D) Hyaluronic acid and chondroitin sulphate

375. The most abundant protein in bones is

(A) Collagen type I

(B) Collagen type II

(D) Non-collagen proteins

376. The most abundant collagen in cartilages

(A) Type I (B) Type II

377. Collagen and elastin have the following

similarity:

(A) Both are triple helices

(B) Both have hydroxyproline residues

(D) Both are glycoproteins

378. Abnormal collagen structure is seen in all

of the following except

(A) I-cell disease

(B) Osteogenesis imperfecta

(D) Ehlers-Danlos sydrome

379. I-cell disease results from absence of the

following from lysosomal enzymes:

(A) Signal sequence

(B) Mannose-6-phosphate

(D) A serine residue

380. In I-cell disease, lysosomal enzymes

(A) Are not synthesised

(B) Are inactive

(D) Cannot reach lysosomes

381. Renal glycosuria occurs due to

(A) Increased filtration of glucose in glomeruli

(B) Increased secretion of glucose by renal

tubular cells

(D) Increased conversion of glycogen into glucose

in tubular cells

382. Haematuria can occur in

(A) Haemolytic anaemia

(B) Mismatched blood transfusion

(D) Stone in urinary tract

383. Haematuria can occur in all of the following

except

(A) Acute glomerulonephritis

(B) Cancer of urinary tract

(D) Mismatched blood transfusion

384. Chyluria can be detected by addition of

the following to the urine:

(A) Sulphosalicylic acid (B) Nitric acid

385. Normal range of serum urea is

(A) 0.6–1.5 mg/dl (B) 9–11 mg/dl

386. Normal range of serum creatinine is

(A) 0.6–1.5 mg/dl (B) 9–11 mg/dl

387. Standard urea clearance is

(A) 54 ml/min (B) 75 ml/min

388. Maximum urea clearance is

(A) 54 ml/min (B) 75 ml/min

389. Average creatinine clearance in an adult

man is about

(A) 54 ml/min (B) 75 ml/min

390. Inulin clearance in an average adult man

is about

(A) 54 ml/min (B) 75 ml/min

Q391. Among the following, a test of tubular

function is

(A) Creatinine clearance

(B) Inulin clearance

(D) PSP excretion test

392. A simple way to assess tubular function

is to withhold food and water for 12

hours and, then, measure

(A) Serum urea

(B) Serum creatinine

(D) Specific gravity of urine

393. Among the following, the most sensitive

indicator of glomerular function is

(A) Serum urea

(B) Serum creatinine

(D) Creatinine clearance

394. All the following statements about inulin

are correct except

(A) It is completely non-toxic

(B) It is completely filtered by glomeruli

(D) It is secreted by tubular cells

395. Non-protein nitrogenous substances in

blood include all of the following except

(A) Urea (B) Uric acid

396. Non-protein nitrogenous substances in

blood are raised in

(A) Starvation

(B) Liver damage

(D) All of these

397. Creatinine clearance is deceased in

(A) Acute tubular necrosis

(B) Acute glomerulonephritis

(D) Myopathies

398. Serum amylase is increased in

(A) Acute parotitis (B) Acute pancreatitis

399. Maximum rise in serum amylase occurs in

(A) Acute parotitis

(B) Acute pancreatitis

(D) Pancreatic cancer

400. Serum lipase is increased in

(A) Acute parotitis (B) Acute pancreatitis

401. Which one of the following metabolites

is not directly produced in the hexose

monophosphate pathway?

(A) Fructose-6-phosphate

(B) Dihydroxy acetone phosphate

(D) Erythrose-4-phosphate

402. Which one of the following statements

concerning glucose-6-phosphate dehydrogenase

deficiency is correct?

(A) Young R.B.Cs, particularly reticulocytes,

contain the highest enzyme activity cells show

less enzyme activity

(B) Glucose-6-P Dehydroglucose deficiency

leads to disfuction of many tissues

single deletion of a large sequence of DNA

in the G-6-PD gene

(D) G-6-PD deficiency is precipitated by ingestion

of drugs such as aspirin

403. The phenomenon of inhibition of glycolysis

by O2 is termed as

(A) Red drop (B) Pasteur effect

404. Seratonin is derived in the body from the

following amino acid:

(A) Phenylalanine (B) Histidine

405. Which amino acid is a lipotropic factor?

(A) Lysine (B) Leucine

406. Which among the following is a nutritionally

essential amino acid for man ?

(A) Alanine (B) Glycine

407. The essential amino acids

(A) Must be supplied in the diet because the

organism has lost the capacity to aminate the

corresponding ketoacids

(B) Must be supplied in the diet because the

human has an impaired ability to synthesize

the carbon chain of the corresponding ketoacids

(D) Are defined as those amino acids which

cannot be synthesized by the organism at a

rate adequate to meet metabolic requirements

408. Which among the following is an essential

amino acid?

(A) Cysteine (B) Leucine

409. Which among the following is a basic

amino acid?

(A) Aspargine (B) Arginine

410. This amino acid cannot have optical

isomers:

(A) Alanine (B) Histidine

411. The amino acid which contains a

guanidine group is

(A) Histidine (B) Arginine

412. GABA(gama amino butyric acid) is

(A) Post-synaptic excitatory transmitter

(B) Post-synaptic inhibitor transmitter

(D) inhibitor of glia-cell function

413. Sulphur-containing amino acid is

(A) Glutathione (B) Chondroitin sulphate

414. The useful reagent for detection of amino

acids is

(A) Molisch reagent

(B) Dichlorophenol Indophenol

(D) Biuret

415. The amino acid which contains an indole

group is

(A) Histidine (B) Arginine

416. Sakaguchi reaction is answered by

(A) Lysine

(B) Ornithine

(D) Arginino succinic acid

417. The pH of an amino acid depends

(A) Optical rotation (B) Dissociation constant

418. When amino acids are treated with neutral

formaldehyde, the pH of the mixture

(A) Is not altered

(B) Increases

(D) First increases then decreases

419. Which among the following has an

imidazole group?

(A) Histidine (B) Tryptophan

420. The amino acid exist as Zwitter ions when

they are in

(A) solid state (B) acidic solution

421. Plasma proteins are isolated by

(A) Salting out (B) Electrophoresis

422. After digestion amino acids

(A) Are absorbed into portal circulation

(B) Are absorbed into lymph

(D) Converted into glucose in the intestine

423. Cysteine has the formula:

(A) CH3SH

(B) H2N—CH2—COOH

(D) S—CH2—CH(NH2)—COOH

S—CH2—CH(NH2)—COOH

424. The compound having the formula

H2N—CO—NH—CH2—CH2—CH2—CH— COOH is

NH2

(A) Lysine (B) Glutamine

425. An amino acid which contains a disulphide

bond is

(A) Lysine (B) Methionine

426. One of the following has a phenolic group:

(A) Histidine (B) Hydroxy lysine

427. An amino acid not containing the usual—

COOH group is

(A) Alanine (B) Tryptophan

428. Branched chain amino acids are

(A) Cysteine and cystine

(B) Tyrosine and Tryptophan

(D) Valine, Leucine and Isoleucine

429. A Zwitter ion is one which has in aqueous

solution:

(A) One positive charge and one negative charge

(B) Two positive charges and one negative charge

charge

(D) No electrical charges at all

430. The amino acid which gives yellow colour

with Ninhydrin in paper chromatography

(A) Tyrosine (B) Proline

431. Hydroxylation of Proline and Lysine in a

protein is effected by

(A) Vitamin B1 (B) Vitamin B2

432. Millon’s test is for identification of

(A) Tyrosine (B) Tryptophan

433. Hopkins-Cole test is for identification of

(A) Tyrosine (B) Tryptophan

434. Collagen is very rich in

(A) Glycine (B) Serine

435. All amino acids are optically active except

(A) Glycine (B) Serine

436. Out of 200 different amino acids form in

nature the number of amino acids present

in protein:

(A) 20 (B) 25

437. Enzyme catalyzed hydrolysis of proteins

produces amino acids of the form:

(A) D (B) L

438. The ionizable groups of amino acids are

at least.

(A) 1 (B) 2

439. The neutral amino acid is

(A) Lysine (B) Proline

440. The amino acid containing hydroxyl

group:

(A) Alanine (B) Isoleucine

441. The sulphur containing amino acid:

(A) Homoserine (B) Serine

442. The basic amino acid:

(A) Glycine (B) Leucine

443. The amino acid which synthesizes many

hormones:

(A) Valine (B) Phenyl alanine

444. Amino acids are insoluble in

(A) Acetic acid (B) Chloroform

445. The major end product of protein nitrogen

metabolism in man is

(A) Glycine (B) Uric acid

446. An amino acid not involved in urea cycle

(A) Arginine (B) Histidine

447. NH3 is detoxified in brain chiefly as

(A) Urea (B) Uric acid

448. In humans, NH3 is detoxified in liver as

(A) Creatinine (B) Uric acid

449. The body protein after eighteen years

(A) Remains unchanged

(B) Is decomposed only slightly at intervals of one

month

(D) Is used only for energy requirement

450. The only known physiological methylating

agents in the animal organism are

(A) Choline and betaine

(B) Choline and ä-adenosyl methionine

(D) Dimehtyl glycine and betaine

451. In the synthesis of 1 molecule of urea in

the Kreb’s Hanseleit cycle, the number of

ATPs required is

(A) 1 (B) 2

452. For biosynthesis of proteins

(A) Amino acids only are required

(B) Amino acids and nucleic acids only are

required

(D) Amino acids, nucleic acids, ATP, GTP,

enzymes and activators are required

453. Transmethylation of guanido acetic acid

gives

(A) Creatine phosphate

(B) Creatinine

(D) n-methyl nicotinamide

454. The 2 energy rich compounds needed for

protein biosynthesis are

(A) ATP and GTP (B) ATP and UTP

455. The following ketoacid is involved in

fixing dietary NH3 into amino acid:

(A) Pyruvate (B) Oxalo acetate

456. The metabolite which sustains urea cycle

(A) Ornithine

(B) Citrulline

(D) n-acetyl glutamate

457. Tetra hydroglolate can be freed from N5

methyl tetrahydrofolate only by

(A) Nor epinephrine (B) Ethanol amine

458. Neogenesis of methyl group is

(A) The availability of methyl group form ä

adenosyl methionine

(B) The availability of methyl group from betaine

hydrofolate with a NAD+ dependent

reductase

(D) Availability of methyl group from methyl B12

459. More creatinine is excreted by

(A) Adult males (B) Adult females

460. A growing peptide in a ribosome can not

be shifted to the adjacent ribosome

because

(A) It is firmly attached

(B) It will get the amino acid cleaved

a shift

(D) The adjacent ribosomes have different

composition

461. The first amino acid incorporated in a

polypeptide in a ribosome of a human is

(A) N formyl methionine (B) Methionine

462. The first amino acid incorporated in a

polypeptide in a ribosome of a bacterium

(A) N formyl methionine (B) Methionine

463. The integrator between the TCA cycle and

urea cycle is

(A) Fumarate (B) Malate

464. Bence jones proteinurial characterized by

(A) Non-heat coagulability

(B) Heat coagulability at 100°C

(D) Precipitation at 25°C

465. Bence Jones proteins may be excreted in

urine of patients suffering from

(A) Tuberculosis (B) Diabetes mellitus

466. Xanthuric acid is an abnormal metabolite

(A) Xanthine (B) Uric acid

467. Two nitrogen atoms of Urea in the urea

cycle come from

(A) NH3

(B) One from NH3 and one from aspartate

(D) One from NH3 and one from alanine

468. Pyruvic acid can be obtained by transamination

of alanine with

(A) á- keto glutaric acid

(B) Acetoacetic acid

(D) Phosphoenol Pyruvic acid

469. In the synthesis of 1 molecule of urea in

the Kreb’s Henseleit cycle the number of

AMPs formed is

(A) 1 (B) 2

470. Formation of melanin from tyrosine

requires the action of

(A) Dopa decarboxylation

(B) Diamine oxidase

(D) Tyrosinase

471. In one of the following the quality of the

protein synthesized is affected:

(A) Diabetes mellitus (B) Gont

472. Citrulline is an intermediate of

(A) TCA cycle (B) Urea cycle

473. The semialdehydes are formed under the

action of enzymes characterised as

(A) Aldolases

(B) Peptidyl lysyl oxidases

(D) Elastases

474. Which of the following statement about

the peptide bond is true?

(A) It is a carbon-carbon bond

(B) It has cis hydrogen and oxygen groups

(D) It has rotational freedom

475. Isoenzymes for a given reaction

(A) Have different spedificities

(B) Have identical affinities for the same substrate

(D) Contain similar ratios of different polypeptide

chains

476. The highest concentration of cystine can

be found in

(A) Melanin (B) Chondroitin sulphate

477. One round of Edman degradation of the

peptide: H2N— Gly—Arg—Lys—Phe—

Asp— COOH would result in which of the

following structures or their phenyl isothiocyanate

derivatives?

(A) H2N—Gly—Arg—COOH + H2N—Lys—

Phe— Asp—COOH

(B) H2N—Gly—Arg—Lys—Phe—COOH + Asp

(D) H2N—Gly—Arg—Lys—COOH + H2N—Phe

—Asp—COOH

478. Which of the following techniques is used

to separate proteins based upon differences

in their mass?

(A) Isoelectric focusing

(B) Dialysis

(D) Western blotting

479. The greatest buffering capacity at

physiologic pH would be provided by a

protein rich in which of the following

amino acids ?

(A) Lysine (B) Histidine

480. Which one of the amino acids could serve

as the best buffer at pH 7?

(A) Glutamic acid (B) Arginine

481. Which one of the following statements

concerning glutamine is correct?

(A) Contains three tetratable groups

(B) Is classified as an acidic amino acid

(D) Migrates to the cathode during electrophoresis

at pH 7.0

482. One of the given example is an amino

acid:

(A) Oh-Lysine (B) Protein

483. The lone pair of electrons at one of the

ring nitrogens in the given amino acid

makes a potential ligand, which is

important in binding the iron atoms in

hemoglobin:

(A) Tryptophan (B) Threonine

484. The amino acid which is not optically

active is

(A) Alanine (B) Glycine

485. Optically active compounds are capable of

(A) Different reactions

(B) Rotating plane of polarized light

(D) None of these

486. The reference compound for absolute configuration

of optically active compound is

(A) Alanine (B) Lactic acid

487. All the standard amino acids except the

following have one chiral ‘c’ atom:

(A) Threonine, Isoleucine

(B) Isoleucine, Alanine

(D) Alanine, Glutamine

488. The role of complement proteins:

(A) Defense

(B) Helps immunity of the body

(D) None of these

489. Optical isomers that are mirror images

and non superimposable are called

(A) Diastereomers (B) Euantiomers

490. Living cells have the unique ability to

synthesize only _________ the form of

optical isomer due to _________.

(A) ‘d’ form, stereospecific enzymes

(B) ‘l’ form stereospecific enzymes

(D) ‘L’ form, DNA

491. Isoelectric pH of an amino acid is that pH

at which it has a

(A) Positive charge (B) Negative charge

492. Albuminoids are similar to

(A) Albumin (B) Globulin

493. Abnormal chain of amino acids in sickle

cells anaemia is

(A) Alpha chain (B) Beta chain

494. In prehepatic jaundice, protein flocculation

test is

(A) Normal/weekly positive

(B) Usually positive

(D) None of these

495. Side chains of all amino acids contain

aromatic rings except

(A) Pheynl alanine (B) Alanine

496. In Nitroprusside test, amino acid cystein

produces

(A) Blue colour complex

(B) Red colour

(D) Purple colour

497. Bonds that are formed between two

cysteine residues is

(A) Disulphide (B) Peptide

498. The acid amide of Aspartic acid is

(A) Glutamine (B) Arginine

499. It is the only amino acid having an

ionizing ‘R’ group with a pK’ near 7 and

is important in the active site of some

enzymes:

(A) Arginine (B) Cystein

500. Hemoglobin has a high content of this

amino acid:

(A) Proline (B) Leucine

501. A hexa peptide with 5 aspartic acid would

have a net charge at pH 7:

(A) Neutral (B) Positive

502. In the genetic disorder of cystinuria, the

patient excretes large quantities of

cystine in their urine and its low solubility

causes crystalline cystine to precipitate as

stones in kidneys. The remedy involves

ingesting Na HCO3. Reaction of this

treatment is

(A) NaHCO2 combines with cystine

(B) NaHCO3 raises the pH above the isoelectric

point of cystine

hydrolysis of cystine to cysteine

(D) None of these

503. In the following reaction, Alanine acts as a

3 3

+ → +

H H

| |

H N – C –COO—— H N – C –COOH

| |

CH CH

(A) Acid (B) Base

504. Amino acids excepting histidine are not

good buffering agents in cell because

(A) They exist as zwitter ions

(B) Their pk and not in the physiological pH of a

cell

unlike the others which have at a different pH

(D) None of these

505. At neutral pH Alanine has the following

structure:

(A) − − 2

H N C COOH

(B) + 3 − −

H N C COO

(D) + 2 − −

H N C COO

506. The amino acids in which the R groups

have a net positive charge at pH 7.0 are

(A) Lysine, Arginine, Histidine

(B) Lysine, Aspargine

(D) Glutamine, Arginine

507. Apolipoproteins are

(A) AI (B) AI1

508. The amino acid which has a pK near 4 and

thus is negatively charged at pH 7 is

(A) Alanine (B) Glutamic acid

509. The side chain of which of the following

amino acid contain sulphur atom?

(A) Methionine (B) Threonine

510. Which of the followings gives a positive

test for Ninhydrin?

(A) Reducing sugars (B) Triglycerides

511. In glutathione (a tripeptide) is present

apart from Glutamic acid and cysteine:

(A) Serine (B) Glycine

512. 2-Amino 3-OH propanoic acid is

(A) Glycine (B) Alanine

513. All amino acids have one asymmetric

carbon atom, except

(A) Arginine (B) Aspargine

514. Number of amino acids present in the

plant, animal and microbial proteins:

(A) 20 (B) 80

515. Immunoglobulins are characterized by their

(A) Heavy chains

(B) Molecular weight

(D) Electrophoretic behaviour

516. The bond in proteins that is not hydrolysed

under usual conditions of denaturation:

(A) Hydrophobic bond (B) Hydrogen bond

517. If the amino group and a carboxylic group

of the amino acid are attached to same

carbon atom, the amino acid is called

(A) Alpha (B) Beta

518. Zymogen is

(A) An intracellular enzyme

(B) Serum enzyme

(D) An inactivated enzyme

519. SGOT level in a adult is

(A) 5–40 units/dl (B) 1–4 units/dl

520. Activity of ceruloplasmin shown in vitro:

(A) Reductase (B) Hydrolase

521. Increased serum alanine during fasting is

due to

(A) Breakdown of muscle proteins

(B) Decreased utilization of non essential amino

acids

(D) Impaired renal function

522. The following 4 amino acids are required

for completion of urea cycle except

(A) Aspartic acid (B) Arginine

523. Number of amino acids present in the

dietary proteins:

(A) 22 (B) 23

524. Urea synthesis takes place in

(A) Blood (B) Liver

525. All followings are ketogenic aminoacids

except

(A) Leucine (B) Isoleucine

526. The amino acid containing an indole ring:

(A) Tryptophan (B) Arginine

527. Histidine is converted to histamine

through the process of

(A) Transamination

(B) Decarboxylation

(D) Urea cycle

528. Physiologically active configuration of

amino acids:

(A) L

(B) D

(D) Neither L nor D

529. Cystine is synthesized from

(A) Cysteine (B) Methionine

530. The major constituent of the proteins of

hair and keratin of skin:

(A) Arginine (B) Cysteine

531. NH3 is removed from brain mainly by

(A) Creatinine formation

(B) Uric acid production

(D) Glutamine formation

532. Mechanism by which NH3 is removed from

the kidneys is

(A) Urea formation

(B) Uric acid formation

(D) None of these

533. Low density plasma proteins are rich in

(A) Chylomicrons (B) Cholesterol

534. Transcortins are

(A) Mucoproteins (B) Glycoproteins

535. Proteins that carries Iron into different

tissues is

(A) Ceruloplasmin (B) Trans cortin

536. Naturally occurring amino acids have

(A) L-Configuration (B) D-Configuration

537. Abnormal chain of aminoacids in sickle

cell anemia is

(A) â-chain (B) â-chain

538. A dietary deficiency of tryptophan and

nicotinate leads to

(A) Beri Beri (B) Xerophthalmia

539. Which one of the following is an essential

amino acid?

(A) Arginine (B) Tyrosine

540. One of the following amino acid is solely

ketogenic:

(A) Lysine (B) Alanine

541. Along with CO2, NH3 and ATP, the amino

acid that is needed in urea cycle is

(A) Alanine (B) Isoleucine

542. Isoelectric pH of an amino acid is that pH

at which it has a

(A) Positive charge (B) Negative charge

543. Which of the following contributes

nitrogen atoms to both purine and

pyrimidine rings?

(A) Aspartate

(B) Carbamoyl phosphate

(D) Glutamine

544. Which amino acid is a lipotropic factor?

(A) Lysine (B) Lecuine

545. Which of the following protein is rich in

cysteine?

(A) Elastine (B) Collagen

546. Which amino acid is present at 6th position

of â-chain of Hbs instead of glutamate in

HbA?

(A) Cysteine (B) Valine

547. The amino acid which contains an indole

group is

(A) Histidine (B) Arginine

548. From two amino acids peptide bond

formation involves removal of one

molecule of

(A) Water (B) Ammonia

549. Polymers of more than 100 amino acids

are termed

(A) Proteins (B) Polypeptides

550. The example of globulins:

(A) Leucosin (B) Tuberin

551. The example of scleroproteins:

(A) Glutamin (B) Giladin

552. The example of phosphoprotein:

(A) Mucin (B) Ovovitellin

553. The example of metalloproteins:

(A) Siderophilin (B) OREES mucoid

554. The example of chromoprotein:

(A) Salmine (B) Catalase

555. Deamination is ______ of amino group.

(A) Removal (B) Addition

556. Proteins produce polypeptides from

proteins by

(A) Oxidizing (B) Reducing

557. Proteins react with biuret reagent which

is suggestive of 2 or more

(A) Hydrogen bonds (B) Peptide bonds

558. The disulphide bond is not broken under

the usual conditions of

(A) Filtration (B) Reduction

559. Insulin is oxidized to separate the protein

molecule into its constituent polypeptide

chains without affecting the other part of

the molecule by the use of

(A) Performic acid (B) Oxalic acid

560. Each hydrogen bond is quite

(A) Weak (B) Strong

561. A coiled structure in which peptide bonds

are folded in regular manner by

(A) Globular proteins (B) Fibrous proteins

562. In many proteins the hydrogen bonding

produces a regular coiled arrangement

called

(A) á-helix (B) â-helix

563. Many globular proteins are stable in

solution although they lack in

(A) Hydrogen bonds (B) Salt bonds

564. Each turn of á-helix contains the number

of amino acids

(A) 2.8 (B) 3.2

565. The distance travelled per turn of á-helix

in nm is

(A) 0.34 (B) 0.44

566. á-helix is disrupted by certain amino

acids like

(A) Proline (B) Arginine

567. á-helix is stabilized by

(A) Hydrogen bonds (B) Disulphide bonds

568. Foetal haemoglobin contains

(A) Two á and two ã chains

(B) Two â and two ã chains

(D) None of these

569. When haemoglobin takes up oxygen

there is a change in the structure due to

the moving closer together of

(A) â-chains (B) â-chains

570. The hydrogen bonds in the secondary and

tertiary structure of proteins are directly

attacked by

(A) Salts (B) Alkalies

571. The hydrogen bonds between peptide

linkages are interfered by

(A) Guanidine (B) Uric acid

572. The digestability of certain denatured

proteins by proteolytic enzymes

(A) Decreases (B) Increases

573. The antigenic antibody functions of

proteins by denaturation are frequently

(A) Not changed (B) Changed

574. In case of severe denaturation of protein,

there is

(A) Reversible denaturation

(B) Moderate reversible denaturation

(D) None of these

575. When egg albumin is heated till it is

coagulated, the secondary and tertiary

structures of the proteins are completely lost

resulting in a mixture of randomly arranged

(A) Dipeptide chains (B) Tripeptide chains

576. In glycoproteins the carbohydrate is in the

form of disaccharide units, the number of

units are

(A) 50–100 (B) 200–300

577. The milk protein in the stomach of the

infants is digested by

(A) Pepsin (B) Trypsin

578. Achylia gastrica is said to be when absence

(A) Pepsin only (B) Both pepsin and HCl

579. The pH of gastric juice become low in

(A) Hemolytic anemia (B) Pernicious anemia

580. In small intestine trypsin hydrolyzes

peptide linkages containing

(A) Arginine (B) Histidine

581. Chymotrypsin in the small intestine

hydrolyzes peptide linkages containing

(A) Alanine (B) Pheynl alanine

582. Carboxy peptidase B in the small

intestine hydrolyzes peptides containing

(A) Leucine (B) Isoleucine

583. The transport of amino acids regulated by

active processes of different numbers:

(A) 1 (B) 2

584. The third active process for amino acids

transport involves

(A) Acidic amino acids

(B) Basic amino acids

(D) Sulphur containing amino acids

585. The neutral amino acids for absorption

need

(A) TPP (B) B6 – PO4

586. If one amino acid is fed excess, the

absorption of another is

(A) Slightly accelerated

(B) Moderately accelerated

(D) Retarded

587. Under normal conditions, food proteins

are generally readily digested upto the

present

(A) 67 to 73 (B) 74 to 81

588. By overheating the nutritional value of

cereal proteins is

(A) Increased (B) Decreased

589. More than half of the protein of the liver

and intestinal mucosa are broken down

and resynthesised in

(A) 10 days (B) 12 days

590. The half-life of antibody protein is about

(A) 4 weeks (B) 3 weeks

591. Protein anabolism is stimulated by

(A) ACTH (B) Testosterone

592. The metabolism of protein is integrated

with that of carbohydrate and fat through

(A) Oxaloacetate (B) Citrate

593. The building up and breaking down of

protoplasm are concerned with the

metabolism of

(A) Carbohydrate (B) Lipid

594. The amino acids abstracted from the liver

are not utilized for repair or special

synthesis but are broken down to

(A) Keto acids (B) Sulphur dioxide

595. The unwanted amino acids abstracted

from the tissues are either used up by the

tissue or in the liver converted into

(A) Ammonia (B) Urea

596. Amino acids provide the nitrogen for the

synthesis of

(A) The bases of the phospholipids

(B) Uric acid

(D) Chondroitin sulphates

597. The metabolism of all proteins ingested

over and above the essential requirements

is called

(A) Exogenous metabolism

(B) Endogenous metabolism

(D) None of these

598. Sulphur containing amino acids after

catabolism produces a substance which

is excreted:

(A) SO2 (B) HNO3

599. Ethereal sulphate is synthesized from the

_________ amino acid.

(A) Neutral (B) Acidic

600. The amino acids required for creatine

formation:

(A) Glycine (B) Arginine

601. In human and other ureotelic organisms,

the end product of amino acid nitrogen

metabolism:

(A) Bile acids (B) Ketone bodies

602. The end product of amino acid nitrogen

metabolism in uricotelic organisms

(reptiles and birds) is

(A) Bilirubin (B) Urea

603. The transaminase activity needs the

coenzyme:

(A) ATP (B) B6 – PO4

604. Transamination is a

(A) Irreversible process(B) Reversible process

605. Most amino acids are substrates for

transamination except

(A) Alanine (B) Threonine

606 Oxidative conversion of many amino

acids to their corresponding -ketoacids

occurs in mammalian:

(A) Liver and kidney (B) Adipose tissue

607. The á-ketoacid is decarboxylated by H2O2

forming a carboxylic acid with one carbon

atom less in the absence of the enzyme:

(A) Catalase (B) Decarboxylase

608. The activity of mammalian L-amino acid

oxidase, an FMN – flavo protein, is quite

(A) Slow (B) Rapid

609. From dietary protein as well as from the

urea present in fluids secreted into the

gastrointestinal tract intestinal bacteria

produce

(A) Carbondioxide

(B) Ammonia

(D) Creatine

610. The symptom of ammonia intoxication

includes

(A) Blurring of vision (B) Constipation

611. Ammonia intoxication symptoms occur

when brain ammonia levels are

(A) Slightly diminished (B) Highly diminished

612. Ammonia production by the kidney is

depressed in

(A) Acidosis (B) Alkalosis

613. Ammonia is excreted as ammonium salts

during metabolic acidosis but the majority

is excreted as

(A) Phosphates (B) Creatine

614. Synthesis of glutamine is accompanied

by the hydrolysis of

(A) ATP (B) ADP

615. In brain, the major metabolism for

removal of ammonia is the formation of

(A) Glutamate (B) Aspartate

616. Carbamoyl phosphate synthetase structure

is marked by change in the presence

(A) N-Acetyl glutamate

(B) N-Acetyl Aspartate

(D) Oxalate

617. The biosynthesis of Urea occurs mainly in

the Liver:

(A) Cytosol

(B) Microsomes

(D) Mitochondria

618. One mol. of Urea is synthesized at the

expense of the _______ mols. of ATP.

(A) 2 (B) 3

619. Urea biosynthesis occurs mainly in the

liver involving the number of amino acids:

(A) 3 (B) 4

620. The normal daily output of Urea through

urine in grams:

(A) 10 to 20 (B) 15 to 25

621. In severe acidosis, the output of urea is

(A) Decreased (B) Slightly increased

622. Uremia occurs in

(A) Cirrhosis of the liver(B) Nephritis

623. Clinical symptom in urea cycle disorder is

(A) Mental retardation (B) Drowsiness

624. The sparing action of methionine is

(A) Tyrosine (B) Cystine

625. NH+

4 aminates glutamate to form

glutamine requiring ATP and

(A) K+ (B) Na+

626. Glutathione is a

(A) Dipeptide (B) Tripeptide

627. All following are conjugated proteins

except

(A) Nucleoproteins (B) Proteoses

628. All á-amino acids have one asymmetric

carbon atom except

(A) Arginine (B) Glycine

629. Number of amino acids present in plants,

animals and microbial proteins:

(A) 20 (B) 80

630. Hydrated density of (HD) lipoproteins is

(A) 0.94 gm/ml

(B) 0.94-1.006 gm/ml

(D) 1.063-1.21 gm/l

631. The bond in proteins that is not broken

under usual conditions of denaturation:

(A) Hydrophobic bond (B) Hydrogen bond

632. Plasma proteins act as

(A) Buffers (B) Immunoglobulins

633. Group that reacts in the Biuret test:

(A) Peptide (B) Amino group

634. In nitroprusside test, amino acid cysteine

produces a:

(A) Red colour (B) Blue colour

635. Protein present in hemoglobin has the

structure known as

(A) Primary (B) Secondary

636. Isoelectric pH of an amino acid is that pH

at which it has a

(A) Positive charge (B) Negative charge

637. Albuminoids are similar to

(A) Albumin (B) Globulin

638. Optical isomers of all aminoacids exist

except

(A) Glycine (B) Arginine

639. Proteins that constitute keratin, collagen

and elastin in body are

(A) Protamines (B) Phosphol proteins

640. Systematic name of lysine is

(A) Amino acetic acid

(B) 2,6 diaminohexanoic acid

(D) 2-Aminopropanoic acid

641. Side chains of all following amino acids

contain aromatic rings except

(A) Phenyl alanine (B) Alanine

642. Abnormal chain of amino acids in sickle

cell anaemia is

(A) Alpha chain (B) Beta chain

643. Number of chains in globin part of normal

Hb:

(A) 1 (B) 2

644. The PH of albumin is

(A) 3.6 (B) 4.7

645. Ninhydrin reaction gives a purple colour

and evolves CO2 with

(A) Peptide bonds (B) Histamine

646. Denaturation of proteins involves

breakdown of

(A) Secondary structure(B) Tertiary structure

647. In denaturation of proteins, the bond

which is not broken:

(A) Disulphide bond (B) Peptide bond

648. The purity of an isolated protein can be

tested by employing various methods.

(A) Solubility curve

(B) Molecular weight

(D) Immuno Ractivity

(E) All of these

649. More than one break in the line or in saturation

curve indicates the following

quality of protein.

(A) Non homogenity (B) Purity

650. A sharp moving boundary is obtained

between the pure solvent and solute

containing layer in

(A) Chromatography

(B) Immuno Reactivity

(D) Solubility curve

651. The antibodies raised against a pure

protein will show only one sharp spike on

this technique:

(A) Solubility curve

(B) Solvent precipitation

(D) Immuno electrophoresis

652. This technique takes the advantage of the

fact that each protein has different pH at

which it is electrically neutral i.e., its

isoelectric pH:

(A) Isoelectric focussing

(B) Immunoel Ectro Phoresis

(D) HPLC

653. The following technique makes use of the

difference in net charges of proteins at a

given pH:

(A) Thin layer chromatography

(B) Ion exchange chromatography

(D) Paper chromatography

654. The ratio of the distance moved by a

compound to the distance moved by the

solvent frent is known as its

(A) PI value (B) Linking number

655. The movement of charged particles

towards one of the electrodes under the

influence of electrical current is

(A) Gel filtration

(B) Molecular sieving

(D) Electrophoresis

656. An anion exchange resin linked to

cellulose backbone is

(A) DEAE cellulose (B) CM cellulose

657. A cation exchange resin linked to cellulose

backbone is

(A) CM-cellulose (B) DEAE cellulose

658. The sorting out of molecules according to

size and shape may be adapted to protein

purification in this technique:

(A) Adsorption chromatography

(B) Gel filtration chromatography

(D) None of these

659. Frequently employed materials for the

adsorption chromatography of proteins

include

(A) High capacity supporting gel

(B) Starch blocks

hydroxy apatite

(D) All of these

660. The solubility of most proteins is lowered

at high salt concentrations is called as

(A) Salting in process (B) Salting out process

661. Phenylalanine, ornithine and methionine

are involved in the biogenesis of

(A) Lysergic acid (B) Reserpine

662. All the following diuretics inhibit the

carbonic anhydrase except

(A) Acetazolamide (B) Bumetanide

663. Protein is a polymer of

(A) Sugars (B) Phenols

664. All the following amino acids are optically

active except

(A) Tryptophane (B) Phenylalanine

665. Proteinous substances which catalyze

biochemical reactions are known as

(A) Activators (B) Catalysts

666. Insulin is a protein which controls

(A) Blood clotting (B) Metabolic pathway

667. Proteins which are responsible for defence

mechanism are called

(A) Antimetabolites (B) Antibodies

668. When the net charge on an amino acid is

zero, the pH is maintained as?

(A) 4.5 (B) 11.2

669. Isoelectric point of amino acids is used for

(A) Crystallisation (B) Precipitation

670. Xanthoproteic test is positive in proteins

containing

(A) Sulphur amino acids

(B) á-Amino acids

(D) Aliphatic amino acids

671. All á-amino acids give positive

(A) Million’s test (B) Biurete test

672. N-terminal amino acids of a polypeptide

are estimated by

(A) Edmann reaction (B) Sanger’s reagent

673. Million’s test is positive for

(A) Phenylalanine (B) Glycine

674. Indole group of tryptophan responses

positively to

(A) Glyoxylic acid (B) Schiff’s reagent

675. Guanidine group of argentine gives

positive test with

(A) Lead acetate

(B) Sakaguchi reagent

(D) Molisch’s reagent

676. Thiol group of cysteine gives red colour

with

(A) Sodium acetate

(B) Lead acetate

(D) Barfoed’s reagent

677. Protein deficiency disease is known as

(A) Cushing’s disease

(B) Fabry’s disease

(D) Kwashiorkor and marasmus

678. A vegetable source of protein is

(A) Egg plant

(B) Soyabean

(D) Devil’s dung

679. Oxaloacetate is converted to aspartic acid

(A) Reductase (B) Oxidase

680. Deficiency of biotin results in decrease in

(A) Amino acid synthesis

(B) Lipid synthesis

(D) Fatty acid synthesis

681. The precursor of bile salts, sex hormones

and vitamin D is

(A) Diosgenin (B) Cholesterol

682 Unsaturated fatty acids is known as

(A) Non-essential fatty acids

(B) Essential fatty acids

(D) Phospholipids

683 Biuret test is specific for

(A) Two peptide linkage

(B) Phenolic group

(D) None of these

684. Most of calcium is present in bone, but 2%

present in soft tissue and the blood is

called

(A) Calcinated blood (B) Solidified blood

685. Calcium present with protein is known as

free while in salt form is called as

(A) Bound (B) Precipitated

686. The following ions help in enzymatic

transfer of phosphate from ATP to pyruvic

acid:

(A) Sodium (B) Calcium

687. International enzyme commission classifies

enzymes into

(A) Three classes (B) Six classes

688. Michaelis – Menten equation is used to

explain the effect of substrate concentration

(A) Carbohydrate (B) Enzyme

689. The pH at which an enzyme has maximum

activity is known as

(A) Isoelectric pH (B) Optimum pH

690. Degradation of proteins to amino acids,

glucose from carbohydrates and fatty

acids from lipids is known as

(A) Anabolism (B) Metabolism

691. During glycolysis of glucose the energy

liberated in the absence of oxygen is

known as

(A) Oxygenesis

(B) Glyconeogenesis

(D) Anaerobic fermentation

692. Deficiency of urea cycle enzymes results

into accumulation of citrulline argininosuccinate

arginine in the liver resulting in increasing

concentration of …….. in the blood.

(A) Calcium (B) Sodium

693. Accumulation of trytophan in blood is

known as

(A) Pompe’s disease (B) Wilson’s disease

694. Lymphocytes are responsible for the formation

(A) Serum (B) Plasma

695. Platelets contain an enzyme which has

important role in clotting in blood. This

enzyme is known as

(A) Cholinesterase (B) Transaminase

696. Treatment of pentoses with a concentrated

mineral acid yields a cyclic aldehyde

known as

(A) Pentaldehyde (B) Cyclopental

697. Isoelectric pH is that pH at which protein

is electrically:

(A) Neutral (B) Anionic

698. About 6.25 g of haemoglobin is produced

and destroyed in the body each day and the

total amount of haemoglobin in a normal

healthy 70 kg weighing male adult is

(A) 250 g (B) 150 g

699. Pancreatic juice contains all of the

following except

(A) Trypsinogen (B) Lipase

700. The milk protein in the stomach in an adult

is digested by

(A) Pepsin (B) Rennin

701. Carboxypeptidase, an enzyme of

pancreatic juice, contains

(A) Mn (B) Zinc

702. The zymogen from trypsinogen of

pancreatic juice is converted to active

trypsin by

(A) Peisin (B) Enterocrinin

703. Inactive zymogens are precursors of all

the following gastrointestinal enzymes

except

(A) Carboxypeptidase (B) Pepsin

Q `q2qw w2 2q w12704. Rennin acts on casein of milk in infants in

presence of

(A) Mg++ (B) Zn++

705. All the following are true about phenylketonuria

except

(A) Deficiency of phenylalanine hydroxylase

(B) Mental retardation

pyruvic acid

(D) Decrease serotonin formation

706. Which of the amino acid produces a

vasodilator on decarboxylation?

(A) Glutamin acid (B) Histidine

707. Neutral amino acid is

(A) Leucine (B) Lysine

708. The amino acid containing hydroxy group:

(A) Glycine (B) Isoleucine

709. The amino acid which synthesizes many

hormornes:

(A) Valine (B) Phenylalanine

710. Insulin degradation of disulfide bond

formation is effected by

(A) Pyruvate dehydrogenase

(B) Xylitol reductase

(D) Xanthine oxidase

711. A protein reacts with biuret reagent which

indicates 2 or more

(A) Blood clotting (B) Peptide bond

712. In many proteins the hydrogen bonding

produces a regular coiled arrangement

which is called as

(A) â-Helix (B) á-Helix

713. The milk protein in the stomach of the

infants is digested by

(A) Pepsin (B) Trypsin

714. Protein anabolism is stimulated by

(A) ACTH (B) Testosterone

715. The number of helices present in a collagen

molecule is

(A) 1 (B) 2

716. Which bond is present in the primary

structure of protein?

(A) Ester (B) Hydrogen

717. Sakaguchi reaction is specific for

(A) Guanidine group (B) Phenolic group

718. With the exception of glycine all amino

acids found in protein are

(A) Isocitrate dehydrogenase

(B) Fumarase

(D) ATPase

719 In protein structure the á-helix and â–

pleated sheets are example of

(A) Primary structure (B) Secondary structure

720. An essential amino acid in man is

(A) Proline (B) Threonine

721. An amino acid that does not form an á–

helix is

(A) Asparagine (B) Tyrosine

722. The protein present in hair is

(A) Elastin (B) Prolamine

723. Plasma protein can be separated by

(A) Salting out with (NH4)2SO4

(B) Ultracentrifugation

(D) All of these

724. RNA does not contain

(A) Uracil

(B) Adenine

(D) Phosphate

725. In mammalian cells, ribosomal RNA is

produced mainly in the

(A) Nucleus

(B) Nucleolus

(D) Golgi apparatus

726. Which co-enzyme is not involved in

oxidative decarboxylation of pyruvic

acid?

(A) TPP (B) Mg++

727. A polymeric unit of starch which has a

branched structure is

(A) Glucose (B) Amylopectin

728 The repeating unit in hyaluronic acid is

(A) Glucuronic acid and Galactosamine

(B) Glucuronic acid are glucosamine

(D) Glucuronic acid and N-acetyl galactosamine

729 The repeating disaccharide unit in

celluslose is

(A) Sucrose (B) Maltose