Biochemistry Questions Pool PDF

MCQ FOR BIOCHEMISTRY 1. A drug which prevents uric acid synthesis by inhibiting the enzyme xanthine oxidase is (A) Aspirin (B) Allopurinol (C) Colchicine (D) Probenecid 2. Which of the following is required for crystallization and storage of...

MCQ FOR BIOCHEMISTRY 1. A drug which prevents uric acid synthesis by inhibiting the enzyme xanthine oxidase is (A) Aspirin (B) Allopurinol (C) Colchicine (D) Probenecid 2. Which of the following is required for crystallization and storage of the hormone insulin? (A) Mn++ (B) Mg++ (C) Ca++ (D) Zn++ 3. Oxidation of which substance in the body yields the most calories (A) Glucose (B) Glycogen (C) Protein (D) Lipids 4. Milk is deficient in which vitamins? (A) Vitamin C (B) Vitamin A (C) Vitamin B2 (D) Vitamin K 5. Milk is deficient of which mineral? (A) Phosphorus (B) Sodium (C) Iron (D) Potassium 6. Synthesis of prostaglandinsis is inhibited by (A) Aspirin (B) Arsenic (C) Fluoride (D) Cyanide 7. HDL is synthesized and secreted from (A) Pancreas (B) Liver (C) Kidney (D) Muscle 8. Which is the cholesterol esters that enter cells through the receptor-mediated endocytosis of lipoproteins hydrolyzed? (A) Endoplasmin reticulum (B) Lysosomes (C) Plasma membrane receptor (D) Mitochondria 9. Which of the following phospholipids is localized to a greater extent in the outer leaflet of the membrane lipid bilayer? (A) Choline phosphoglycerides (B) Ethanolamine phosphoglycerides (C) Inositol phosphoglycerides (D) Serine phosphoglycerides 10. All the following processes occur rapidly in the membrane lipid bilayer except (A) Flexing of fatty acyl chains (B) Lateral diffusion of phospholipids (C) Transbilayer diffusion of phopholipids (D) Rotation of phospholipids around their long axes 11. Which of the following statement is correct about membrane cholesterol? (A) The hydroxyl group is located near the centre of the lipid layer (B) Most of the cholesterol is in the form of a cholesterol ester (C) The steroid nucleus form forms a rigid, planar structure (D) The hydrocarbon chain of cholesterol projects into the extracellular fluid 12. Which one is the heaviest particulate component of the cell? (A) Nucleus (B) Mitochondria (C) Cytoplasm (D) Golgi apparatus 13. Which one is the largest particulate of the cytoplasm? (A) Lysosomes (B) Mitochondria (C) Golgi apparatus (D) Entoplasmic reticulum 14. The degradative Processes are categorized under the heading of (A) Anabolism (B) Catabolism (C) Metabolism (D) None of the above 15. 15. The exchange of material takes place (A) Only by diffusion (B) Only by active transport (C) Only by pinocytosis (D) All of these 16. The average pH of Urine is (A) 7.0 (B) 6.0 (C) 8.0 (D) 1.0 17. The pH of blood is 7.4 when the ratio between H2CO3 and NaHCO3 is (A) 1 : 10 (B) 1 : 20 (C) 1 : 25 (D) 1 : 30 18. The phenomenon of osmosis is opposite to that of (A) Diffusion (B) Effusion (C) Affusion (D) Coagulation 19. The surface tension in intestinal lumen between fat droplets and aqueous medium is decreased by (A) Bile Salts (B) Bile acids (C) Conc. H2SO4 (D) Acetic acid 20. Which of the following is located in the mitochondria? (A) Cytochrome oxidase (B) Succinate dehydrogenase (C) Dihydrolipoyl dehydrogenase (D) All of these 21. The most active site of protein synthesis is the (A) Nucleus (B) Ribosome (C) Mitochondrion (D) Cell sap 22. The fatty acids can be transported into and out of mitochondria through (A) Active transport (B) Facilitated transfer (C) Non-facilitated transfer (D) None of these 23. Mitochondrial DNA is (A) Circular double stranded (B) Circular single stranded (C) Linear double helix (D) None of these 24. The absorption of intact protein from the gut in the fetal and newborn animals takes place by (A) Pinocytosis (B) Passive diffusion (C) Simple diffusion (D) Active transport 25. The cellular organelles called “suicide bags” are (A) Lysosomes  (B) Ribosomes (C) Nucleolus (D) Golgi’s bodies 26. From the biological viewpoint, solutions can be grouped into (A) Isotonic solution (B) Hypotonic solutions (C) Hypertonic solution (D) All of these 27. Bulk transport across cell membrane is accomplished by (A) Phagocytosis (B) Pinocytosis (C) Extrusion (D) All of these 28. The ability of the cell membrane to act as a selective barrier depends upon (A) The lipid composition of the membrane (B) The pores which allows small molecules (C) The special mediated transport systems (D) All of these 29. Carrier protein can (A) Transport only one substance (B) Transport more than one substance (C) Exchange one substance to another (D) Perform all of these functions 30. A lipid bilayer is permeable to (A) Urea (B) Fructose (C) Glucose (D) Potassium 31. The Golgi complex (A) Synthesizes proteins (B) Produces ATP (C) Provides a pathway for transporting chemicals (D) Forms glycoproteins 32. The following points about microfilaments are true except (A) They form cytoskeleton with microtubules (B) They provide support and shape (C) They form intracellular conducting channels (D) They are involved in muscle cell contraction 33. The following substances are cell inclusions except (A) Melanin (B) Glycogen (C) Lipids (D) Centrosome 34. Fatty acids can be transported into and out of cell membrane by (A) Active transport  (B) Facilitated transport (C) Diffusion (D) Osmosis 35. Enzymes catalyzing electron transport are present mainly in the (A) Ribosomes (B) Endoplasmic reticulum (C) Lysosomes (D) Inner mitochondrial membrane 36. Mature erythrocytes do not contain (A) Glycolytic enzymes (B) HMP shunt enzymes (C) Pyridine nucleotide (D) ATP 37. In mammalian cells rRNA is produced mainly in the (A) Endoplasmic reticulum (B) Ribosome (C) Nucleolus (D) Nucleus 38. Genetic information of nuclear DNA is transmitted to the site of protein synthesis by (A) rRNA (B) mRNA (C) tRNA (D) Polysomes 39. The power house of the cell is (A) Nucleus (B) Cell membrane (C) Mitochondria (D) Lysosomes 40. The digestive enzymes of cellular compounds are confined to (A) Lysosomes (B) Ribosomes (C) Peroxisomes (D) Polysomes 41. The general formula of monosaccharide is (A) CnH2nOn (B) C2nH2On (C) CnH2O2n (D) CnH2nO2n 42. The general formula of polysaccharides is (A) (C6H10O5)n (B) (C6H12O5)n (C) (C6H10O6)n (D) (C6H10O6)n 43. The aldose sugar is (A) Glycerose  (B) Ribulose (C) Erythrulose (D) Dihydoxyacetone 44. A triose sugar is (A) Glycerose (B) Ribose (C) Erythrose (D) Fructose 45. A pentose sugar is (A) Dihydroxyacetone (B) Ribulose (C) Erythrose (D) Glucose 46. The pentose sugar present mainly in the heart muscle is (A) Lyxose (B) Ribose (C) Arabinose (D) Xylose 47. Polysaccharides are (A) Polymers (B) Acids (C) Proteins (D) Oils 48. The number of isomers of glucose is (A) 2 (B) 4 (C) 8 (D) 16 49. Two sugars which differ from one another only in configuration around a single carbon atom are termed (A) Epimers (B) Anomers (C) Optical isomers (D) Stereoisomers 50. Isomers differing as a result of variations in configuration of the —OH and —H on carbon atoms 2, 3 and 4 of glucose are known as (A) Epimers (B) Anomers (C) Optical isomers (D) Steroisomers 51. The most important epimer of glucose is (A) Galactose  (B) Fructose (C) Arabinose (D) Xylose 52. The α-D-glucose and β-D-glucose are (A) Stereoisomers (B) Epimers (C) Anomers (D) Keto-aldo pairs 53. The α-D-glucose + 1120 → + 52.50 ← + 190 β- D-glucose for glucose above represents (A) Optical isomerism (B) Mutarotation (C) Epimerisation (D) D and L isomerism 54. Compounds having the same structural formula but differing in spatial configuration are known as (A) Stereoisomers (B) Anomers (C) Optical isomers (D) Epimers 55. In glucose the orientation of the —H and —OH groups around the carbon atom 5 adjacent to the terminal primary alcohol carbon determines (A) D or L series (B) Dextro or levorotatory (C) alpha and beta anomers (D) Epimers 56. The carbohydrate of the blood group substances is (A) Sucrose (B) Fucose (C) Arabinose (D) Maltose 57. The Erythromycin contains (A) Dimethyl amino sugar (B) Trimethyl amino sugar (C) Sterol and sugar (D) Glycerol and sugar 58. A sugar alcohol is (A) Mannitol (B) Trehalose (C) Xylulose (D) Arabinose 59. The major sugar of insect hemolymph is (A) Glycogen (B) Pectin (C) Trehalose (D) Sucrose 60. The sugar found in DNA is (A) Xylose (B) Ribose (C) Deoxyribose (D) Ribulose 61. The sugar found in RNA is (A) Ribose (B) Deoxyribose (C) Ribulose (D) Erythrose 62. The sugar found in milk is (A) Galactose (B) Glucose (C) Fructose (D) Lactose 63. Invert sugar is (A) Lactose (B) Sucrose (C) Hydrolytic products of sucrose (D) Fructose 64. Sucrose consists of (A) Glucose + glucose (B) Glucose + fructose (C) Glucose + galactose (D) Glucose + mannose 65. The monosaccharide units are linked by 1 → 4 glycosidic linkage in (A) Maltose (B) Sucrose (C) Cellulose (D) Cellobiose 66. Which of the following is a non-reducing sugar? (A) Isomaltose (B) Maltose (C) Lactose  (D) Trehalose 67. Which of the following is a reducing sugar? (A) Sucrose (B) Trehalose (C) Isomaltose (D) Agar 68. A dissaccharide formed by 1,1-glycosidic linkage between their monosaccharide units is (A) Lactose (B) Maltose (C) Trehalose (D) Sucrose 69. A dissaccharide formed by 1,1-glycosidic linkage between their monosaccharide units is (A) Lactose (B) Maltose (C) Trehalose (D) Sucrose 70. Mutarotation refers to change in (A) pH (B) Optical rotation (C) Conductance (D) Chemical properties 71. A polysacchharide which is often called animal starch is (A) Glycogen (B) Starch (C) Inulin (D) Dextrin 72. The homopolysaccharide used for intravenous infusion as plasma substitute is (A) Agar (B) Inulin (C) Pectin (D) Starch 73. The polysaccharide used in assessing the glomerular filtration rate (GFR) is (A) Glycogen (B) Agar (C) Inulin (D) Hyaluronic acid 74. The constituent unit of inulin is (A) Glucose (B) Fructose  (C) Mannose (D) Galactose 75. The polysaccharide found in the exoskeleton of invertebrates is (A) Pectin (B) Chitin (C) Cellulose (D) Chondroitin sulphate 76. Which of the following is a heteroglycan? (A) Dextrins (B) Agar (C) Inulin (D) Chitin 77. The glycosaminoglycan which does not contain uronic acid is (A) Dermatan sulphate (B) Chondroitin sulphate (C) Keratan sulphate (D) Heparan sulphate 78. The glycosaminoglycan which does not contain uronic acid is (A) Hyaluronic acid (B) Heparin (C) Chondroitin sulphate (D) Dermatan sulphate 79. Keratan sulphate is found in abundance in (A) Heart muscle (B) Liver (C) Adrenal cortex (D) Cornea 80. Repeating units of hyaluronic acid are (A) N-acetyl glucosamine and D-glucuronic acid (B) N-acetyl galactosamine and D-glucuronic acid (C) N-acetyl glucosamine and galactose (D) N-acetyl galactosamine and L- iduronic acid 81. The approximate number of branches in amylopectin is (A) 10 (B) 20 (C) 40 (D) 80 82. In amylopectin the intervals of glucose units of each branch is (A) 10–20  (B) 24–30 (C) 30–40 (D) 40–50 83. A polymer of glucose synthesized by the action of leuconostoc mesenteroids in a sucrose medium is (A) Dextrans (B) Dextrin (C) Limit dextrin (D) Inulin 84. Glucose on reduction with sodium amalgam forms (A) Dulcitol (B) Sorbitol (C) Mannitol (D) Mannitol and sorbitol 85. Glucose on oxidation does not give (A) Glycoside (B) Glucosaccharic acid (C) Gluconic acid (D) Glucuronic acid 86. Oxidation of galactose with conc HNO3 yields (A) Mucic acid (B) Glucuronic acid (C) Saccharic acid (D) Gluconic acid 87. A positive Benedict’s test is not given by (A) Sucrose (B) Lactose (C) Maltose (D) Glucose 88. The Starch is a (A) Polysaccharide (B) Monosaccharide (C) Disaccharide (D) None of these 89. A positive Seliwanoff’s test is obtained with (A) Glucose (B) Fructose (C) Lactose (D) Maltose 90. Osazones are not formed with the  (A) Glucose (B) Fructose (C) Sucrose (D) Lactose 91. The most abundant carbohydrate found in nature is (A) Starch (B) Glycogen (C) Cellulose (D) Chitin 92. Impaired renal function is indicated when the amount of PSP excreted in the first 15 minutes is (A) 20% (B) 35% (C) 40% (D) 45% 93. An early feature of renal disease is (A) Impairment of the capacity of the tubule to perform osmotic work (B) Decrease in maximal tubular excretory capacity (C) Decrease in filtration factor (D) Decrease in renal plasma flow 94. ADH test is based on the measurement of (A) Specific gravity of urine (B) Concentration of urea in urine (C) Concentration of urea in blood (D) Volume of urine in ml/minute 95. The specific gravity of urine normally ranges from (A) 0.900–0.999 (B) 1.003–1.030 (C) 1.000–1.001 (D) 1.101–1.120 96. Specific gravity of urine increases in (A) Diabetes mellitus (B) Chronic glomerulonephritis (C) Compulsive polydypsia (D) Hypercalcemia 97. Fixation of specific gravity of urine to 1.010 is found in (A) Diabetes insipidus (B) Compulsive polydypsia (C) Cystinosis (D) Chronic glomerulonephritis 98. Addis test is the measure of (A) Impairment of the capacity of the tubule to perform osmotic work (B) Secretory function of liver (C) Excretory function of liver (D) Activity of parenchymal cells of liver 99. Number of stereoisomers of glucose is (A) 4 (B) 8 (C) 16 (D) None of these 100. Maltose can be formed by hydrolysis of (A) Starch (B) Dextrin (C) Glycogen (D) All of these 101. The α –D–Glucuronic acid is present in (A) Hyaluronic acid (B) Chondroitin sulphate (C) Heparin (D) All of these 102. Fructose is present in hydrolysate of (A) Sucrose (B) Inulin (C) Both of the above (D) None of these 103. A carbohydrate found in DNA is (A) Ribose (B) Deoxyribose (C) Ribulose (D) All of these 104. Ribulose is a these (A) Ketotetrose (B) Aldotetrose (C) Ketopentose (D) Aldopentose 105. A carbohydrate, commonly known as dextrose is (A) Dextrin (B) D-Fructose (C) D-Glucose  (D) Glycogen 106. A carbohydrate found only in milk is (A) Glucose (B) Galactose (C) Lactose (D) Maltose 107. A carbohydrate, known commonly as invert sugar, is (A) Fructose (B) Sucrose (C) Glucose (D) Lactose 108. A heteropolysacchraide among the following is (A) Inulin (B) Cellulose (C) Heparin (D) Dextrin 109. The predominant form of glucose in solution is (A) Acyclic form (B) Hydrated acyclic form (C) Glucofuranose (D) Glucopyranose 110. An L-isomer of monosaccharide formed in human body is (A) L-fructose (B) L-Erythrose (C) L-Xylose (D) L-Xylulose 111. Hyaluronic acid is found in (A) Joints (B) Brain (C) Abdomen (D) Mouth 112. The carbon atom which becomes asymmetric when the straight chain form of monosaccharide changes into ring form is known as (A) Anomeric carbon atom (B) Epimeric carbon atom (C) Isomeric carbon atom (D) None of these 113. The smallest monosaccharide having furanose ring structure is (A) Erythrose  (B) Ribose (C) Glucose (D) Fructose 114. Which of the following is an epimeric pair? (A) Glucose and fructose (B) Glucose and galactose (C) Galactose and mannose (D) Lactose and maltose 115. α-Glycosidic bond is present in (A) Lactose (B) Maltose (C) Sucrose (D) All of these 116. Branching occurs in glycogen approximately after every (A) Five glucose units (B) Ten glucose units (C) Fifteen glucose units (D) Twenty glucose units 117. N–Acetylglucosamnine is present in (A) Hyaluronic acid (B) Chondroitin sulphate (C) Heparin (D) All of these 118. Iodine gives a red colour with (A) Starch (B) Dextrin (C) Glycogen (D) Inulin 119. Amylose is a constituent of (A) Starch (B) Cellulose (C) Glycogen (D) None of these 120. Synovial fluid contains (A) Heparin (B) Hyaluronic acid (C) Chondroitin sulphate (D) Keratin sulphate 121. Gluconeogenesis is decreased by  (A) Glucagon (B) Epinephrine (C) Glucocorticoids (D) Insulin 122. Lactate formed in muscles can be utilized through (A) Rapoport-Luebeling cycle (B) Glucose-alanine cycle (C) Cori’s cycle (D) Citric acid cycle 123. Glucose-6-phosphatase is not present in (A) Liver and kidneys (B) Kidneys and muscles (C) Kidneys and adipose tissue (D) Muscles and adipose tissue 124. Pyruvate carboxylase is regulated by (A) Induction (B) Repression (C) Allosteric regulation (D) All of these 125. Fructose-2, 6-biphosphate is formed by the action of (A) Phosphofructokinase-1 (B) Phosphofructokinase-2 (C) Fructose biphosphate isomerase (D) Fructose-1, 6-biphosphatase 126. The highest concentrations of fructose are found in (A) Aqueous humor (B) Vitreous humor (C) Synovial fluid (D) Seminal fluid 127. Glucose uptake by liver cells is (A) Energy-consuming (B) A saturable process (C) Insulin-dependent (D) Insulin-independent 128. Renal threshold for glucose is decreased in (A) Diabetes mellitus (B) Insulinoma (C) Renal glycosuria (D) Alimentary glycosuria 129. Active uptake of glucose is inhibited by (A) Ouabain (B) Phlorrizin (C) Digoxin (D) Alloxan 130. Glucose-6-phosphatase is absent or deficient in (A) Von Gierke’s disease (B) Pompe’s disease (C) Cori’s disease (D) McArdle’s disease 131. Debranching enzyme is absent in (A) Cori’s disease (B) Andersen’s disease (C) Von Gierke’s disease (D) Her’s disease 132. McArdle’s disease is due to the deficiency of (A) Glucose-6-phosphatase (B) Phosphofructokinase (C) Liver phosphorylase (D) Muscle phosphorylase 133. Tautomerisation is (A) Shift of hydrogen (B) Shift of carbon (C) Shift of both (D) None of these 134. In essential pentosuria, urine contains (A) D-Ribose (B) D-Xylulose (C) L-Xylulose (D) D-Xylose 135. Action of salivary amylase on starch leads to the formation of (A) Maltose (B) Maltotriose (C) Both of the above (D) Neither of these 136. Congenital galactosaemia can lead to (A) Mental retardation (B) Premature cataract (C) Death  (D) All of the above 137. Uridine diphosphate glucose (UDPG) is (A) Required for metabolism of galactose (B) Required for synthesis of glucuronic acid (C) A substrate for glycogen synthetase (D) All of the above 138. Catalytic activity of salivary amylase requires the presence of (A) Chloride ions (B) Bromide ions (C) Iodide ions (D) All of these 139. The following is actively absorbed in the intestine: (A) Fructose (B) Mannose (C) Galactose (D) None of these 140. An amphibolic pathway among the following is (A) HMP shunt (B) Glycolysis (C) Citirc acid cycle (D) Gluconeogenesis 141. Cori’s cycle transfers (A) Glucose from muscles to liver (B) Lactate from muscles to liver (C) Lactate from liver to muscles (D) Pyruvate from liver to muscles 142. During starvation, ketone bodies are used as a fuel by (A) Erythrocytes (B) Brain (C) Liver (D) All of these 143. The following is an enzyme required for glycolysis: (A) Pyruvate kinase (B) Pyruvate carboxylase (C) Glucose-6-phosphatase (D) Glycerokinase 144. Our body can get pentoses from (A) Glycolytic pathway (B) Uromic acid pathway  (C) TCA cycle (D) HMP shunt 145. Conversion of glucose to glucose-6- phosphate in human liver is by (A) Hexokinase only (B) Glucokinase only (C) Hexokinase and glucokinase (D) Glucose-6-phosphate dehydrogenase 146. The following is an enzyme required for glycolysis: (A) Pyruvate kinase (B) Pyruvate carboxylase (C) Glucose-6-phosphatose (D) Glycerokinase 147. Under anaerobic conditions the glycolysis of one mole of glucose yields ______moles of ATP. (A) One (B) Two (C) Eight (D) Thirty 148. Glycogen is converted to glucose-1- phosphate by (A) UDPG transferase (B) Branching enzyme (C) Phosphorylase (D) Phosphatase 149. Which of the following is not an enzyme involved in glycolysis? (A) Euolase (B) Aldolose (C) Hexokinase (D) Glucose oxidase 150. Tricarboxylic acid cycle to be continuous requires the regeneration of (A) Pyruvic acid (B) oxaloacetic acid (C) α-oxoglutaric acid (D) Malic acid 151. Two examples of substrate level phosphorylation I EM pathway of glucose metabolism are in the reactions of (A) 1,3 bisphosphoglycerate and phosphoenol pyruvate (B) Glucose-6 phosphate and Fructo-6-phosphate (C) 3 phosphoglyceraldehyde and phosphoenolpyruvate (D) 1,3 diphosphoglycerate and 2-phosphoglycerate 152. The number of molecules of ATP produced by the total oxidation of acetyl CoA in TCA cycle is  (A) 6 (B) 8 (C) 10 (D) 12 153. Substrate level phosphorylation in TCA cycle is in step: (A) Isocitrate dehydrogenase (B) Malate dehydrogenase (C) Aconitase (D) Succinate thiokinase 154. Fatty acids cannot be converted into carbohydrates in the body as the following reaction is not possible. (A) Conversion of glucose-6-phosphate into glucose (B) Fructose 1, 6-bisphosphate to fructose-6-phosphate (C) Transformation of acetyl CoA to pyruvate (D) Formation of acetyl CoA from fatty acids 155. Starch and glycogen are polymers of (A) Fructose (B) Mannose (C) α−D-Glucose (D) Galactose 156. Reducing ability of carbohydrates is due to (A) Carboxyl group (B) Hydroxyl group (C) Enediol formation (D) Ring structure 157. Which of the following is not a polymer of glucose? (A) Amylose (B) Inulin (C) Cellulose (D) Dextrin 158. Invert sugar is (A) Lactose (B) Mannose (C) Fructose (D) Hydrolytic product of sucrose 159. The carbohydrate reserved in human body is (A) Starch (B) Glucose (C) Glycogen  (D) Inulin 160. A disaccharide linked by α -1-4 Glycosidic linkage is (A) Lactose (B) Sucrose (C) Cellulose (D) Maltose 161. All proteins contain the (A) Same 20 amino acids (B) Different amino acids (C) 300 Amino acids occurring in nature (D) Only a few amino acids 162. Proteins contain (A) Only L- α - amino acids (B) Only D-amino acids (C) DL-Amino acids (D) Both (A) and (B) 163. The optically inactive amino acid is (A) Glycine (B) Serine (C) Threonine (D) Valine 164. At neutral pH, a mixture of amino acids in solution would be predominantly: (A) Dipolar ions (B) Nonpolar molecules (C) Positive and monovalent (D) Hydrophobic 165. 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 (C) Some amino acids contain only positive charge (D) All amino acids contain negatively charged side chains 166. pH (isoelectric pH) of alanine is (A) 6.02 (B) 6.6 (C) 6.8 (D) 7.2 167. 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  (C) 5.9 (D) 6.0 168. Sulphur containing amino acid is (A) Methionine (B) Leucine (C) Valine (E) Asparagine 169. An example of sulphur containing amino acid is (A) 2-Amino-3-mercaptopropanoic acid (B) 2-Amino-3-methylbutanoic acid (C) 2-Amino-3-hydroxypropanoic acid (D) Amino acetic acid 170. All the following are sulphur containing amino acids found in proteins except (A) Cysteine (B) Cystine (C) Methionine (D) Threonine 171. An aromatic amino acid is (A) Lysine (B) Tyrosine (C) Taurine (D) Arginine 172. The functions of plasma albumin are (A) Osmosis (B) Transport (C) Immunity (D) both (A )and (B) 173. Amino acid with side chain containing basic groups is (A) 2-Amino 5-guanidovaleric acid (B) 2-Pyrrolidine carboxylic acid (C) 2-Amino 3-mercaptopropanoic acid (D) 2-Amino propanoic acid 174. An example of α-amino acid not present in proteins but essential in mammalian metabolism is (A) 3-Amino 3-hydroxypropanoic acid (B) 2-Amino 3-hydroxybutanoic acid (C) 2-Amino 4-mercaptobutanoic acid (D) 2-Amino 3-mercaptopropanoic acid 175. An essential amino acid in man is (A) Aspartate  (B) Tyrosine (C) Methionine (D) Serine 176. Non essential amino acids (A) Are not components of tissue proteins (B) May be synthesized in the body from essential amino acids (C) Have no role in the metabolism (D) May be synthesized in the body in diseased states 177. Which one of the following is semi essential amino acid for humans? (A) Valine (B) Arginine (C) Lysine (D) Tyrosine 178. An example of polar amino acid is (A) Alanine (B) Leucine (C) Arginine (D) Valine 179. The amino acid with a nonpolar side chain is (A) Serine (B) Valine (C) Asparagine (D) Threonine 180. A ketogenic amino acid is (A) Valine (B) Cysteine (C) Leucine (D) Threonine 181. An amino acid that does not form an α-helix is (A) Valine (B) Proline (C) Tyrosine (D) Tryptophan 182. An amino acid not found in proteins is (A) β-Alanine (B) Proline (C) Lysine (D) Histidine 183. In mammalian tissues serine can be a biosynthetic precursor of  (A) Methionine (B) Glycine (C) Tryptophan (D) Phenylalanine 184. A vasodilating compound is produced by the decarboxylation of the amino acid: (A) Arginine (B) Aspartic acid (C) Glutamine (D) Histidine 185. Biuret reaction is specific for (A) –CONH-linkages (B) –CSNH2 group (C) –(NH)NH2 group (D) All of these 186. Sakaguchi’s reaction is specific for (A) Tyrosine (B) Proline (C) Arginine (D) Cysteine 187. Million-Nasse’s reaction is specific for the amino acid: (A) Tryptophan (B) Tyrosine (C) Phenylalanine (D) Arginine 188. Ninhydrin with evolution of CO2 forms a blue complex with (A) Peptide bond (B) α -Amino acids (C) Serotonin (D) Histamine 189. The most of the ultraviolet absorption of proteins above 240 nm is due to their content of (A) Tryptophan (B) Aspartate (C) Glutamate (D) Alanine 190. Which of the following is a dipeptide? (A) Anserine (B) Glutathione (C) Glucagon (D) Lipoprotein 191. Which of the following is a tripeptide? (A) Anserine (B) Oxytocin (C) Glutathione (D) Kallidin 192. A peptide which acts as potent smooth muscle hypotensive agent is (A) Glutathione (B) Bradykinin (C) Tryocidine (D) Gramicidin-s 193. A tripeptide functioning as an important reducing agent in the tissues is (A) Bradykinin (B) Kallidin (C) Tyrocidin (D) Glutathione 194. An example of metalloprotein is (A) Casein (B) Ceruloplasmin (C) Gelatin (D) Salmine 195. Carbonic anhydrase is an example of (A) Lipoprotein (B) Phosphoprotein (C) Metalloprotein (D) Chromoprotein 196. An example of chromoprotein is (A) Hemoglobin (B) Sturine (C) Nuclein (D) Gliadin 197. An example of scleroprotein is (A) Zein (B) Keratin (C) Glutenin (D) Ovoglobulin 198. Casein, the milk protein is (A) Nucleoprotein (B) Chromoprotein (C) Phosphoprotein  (D) Glycoprotein 199. An example of phosphoprotein present in egg yolk is (A) Ovoalbumin (B) Ovoglobulin (C) Ovovitellin (D) Avidin 200. A simple protein found in the nucleoproteins of the sperm is (A) Prolamine (B) Protamine (C) Glutelin (D) Globulin 201. Histones are (A) Identical to protamine (B) Proteins rich in lysine and arginine (C) Proteins with high molecular weight (D) Insoluble in water and very dilute acids 202. The protein present in hair is (A) Keratin (B) Elastin (C) Myosin (D) Tropocollagen 203. The amino acid from which synthesis of the protein of hair keratin takes place is (A) Alanine (B) Methionine (C) Proline (D) Hydroxyproline 204. In one molecule of albumin the number of amino acids is (A) 510 (B) 590 (C) 610 (D) 650 205. Plasma proteins which contain more than 4% hexosamine are (A) Microglobulins (B) Glycoproteins (C) Mucoproteins (D) Orosomucoids 206. After releasing O2 at the tissues, hemoglobin transports (A) CO2 and protons to the lungs (B) O2 to the lungs  (C) CO2 and protons to the tissue (D) Nutrients 207. Ehlers-Danlos syndrome characterized by hypermobile joints and skin abnormalities is due to (A) Abnormality in gene for procollagen (B) Deficiency of lysyl oxidase (C) Deficiency of prolyl hydroxylase (D) Deficiency of lysyl hydroxylase 208. Proteins are soluble in (A) Anhydrous acetone (B) Aqueous alcohol (C) Anhydrous alcohol (D) Benzene 209. A cereal protein soluble in 70% alcohol but insoluble in water or salt solution is (A) Glutelin (B) Protamine (C) Albumin (D) Gliadin 210. Many globular proteins are stable in solution inspite they lack in (A) Disulphide bonds (B) Hydrogen bonds (C) Salt bonds (D) Non polar bonds 211. The hydrogen bonds between peptide linkages of a protein molecules are interfered by (A) Guanidine (B) Uric acid (C) Oxalic acid (D) Salicylic acid 212. 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 (C) Greater than 10 and generally 20 (D) Greater than 10 213. Fibrous proteins have axial ratio (A) Less than 10 (B) Less than 10 and generally not greater than 3–4 (C) Generally 10 (D) Greater than 10 214. Each turn of α -helix contains the amino acid residues (number):  (A) 3.6 (B) 3.0 (C) 4.2 (D) 4.5 215. Distance traveled per turn of alpha helix in nm is (A) 0.53 (B) 0.54 (C) 0.44 (D) 0.48 216. Along the alpha-helix each amino acid residue advances in nm by (A) 0.15 (B) 0.10 (C) 0.12 (D) 0.20 217. The number of helices present in a collagen molecule is (A) 1 (B) 2 (C) 3 (D) 4 218. In proteins the alpha-helix and beta-pleated sheet are examples of (A) Primary structure (B) Secondary structure (C) Tertiary structure (D) Quaternary structure 219. The a-helix of proteins is (A) A pleated structure (B) Made periodic by disulphide bridges (C) A non-periodic structure (D) Stabilised by hydrogen bonds between NH and CO groups of the main chain 220. At the lowest energy level alpha-helix of polypeptide chain is stabilized (A) By hydrogen bonds formed between the H of peptide N and the carbonyl O of the residue (B) Disulphide bonds (C) Non polar bonds (D) Ester bonds 221. Both alpha-helix and beta-pleated sheet conformation of proteins were proposed by (A) Watson and Crick (B) Pauling and Corey (C) Waugh and King  (D) Y.S.Rao 222. The primary structure of fibroin, the principal protein of silk worm fibers consists almost entirely of (A) Glycine (B) Aspartate (C) Keratin (D) Tryptophan 223. Tertiary structure of a protein describes (A) The order of amino acids (B) Location of disulphide bonds (C) Loop regions of proteins (D) The ways of protein folding 224. In a protein molecule the disulphide bond is not broken by (A) Reduction (B) Oxidation (C) Denaturation (D) X-ray diffraction 225. The technique for purification of proteins that can be made specific for a given protein is (A) Gel filtration chromatography (B) Ion exchange chromatography (C) Electrophoresis (D) Affinity chromatography 226. Denaturation of proteins results in (A) Disruption of primary structure (B) Breakdown of peptide bonds (C) Destruction of hydrogen bonds (D) Irreversible changes in the molecule 227. Ceruloplasmin is (A) alpha 1-globulin (B) alpha 2-globulin (C) beta-globulin (D) None of these 228. The lipoprotein with the fastest electrophoretic mobility and the lowest triglyceride content is (A) Chylomicron (B) VLDL (C) IDL (D) HDL 229. The lipoprotein associated with activation of LCAT is (A) HDL  (B) LDL (C) VLDL (D) IDL 230. The apolipoprotein which acts as activator of LCAT is (A) A-I (B) A-IV (C) C-II (D) D 231. The Apo lipoprotein which acts as activator of extra hepatic lipoprotein is (A) Apo-A (B) Apo-B (C) Apo-C (D) Apo-D 232. The apo lipoprotein which forms the integral component of chylomicron is (A) B-100 (B) B-48 (C) C (D) D 233. The apo lipoprotein which from the integral component of VLDL is (A) B-100 (B) B-48 (C) A (D) D 234. The apo lipoprotein which acts as ligand for LDL receptor is (A) B-48 (B) B-100 (C) A (D) C 235. Serum LDL has been found to be increased in (A) Obstructive jaundice (B) Hepatic jaundice (C) Hemolytic jaundice (D) Malabsorption syndrome 236. A lipoprotein associated with high incidence of coronary atherosclerosis is (A) LDL (B) VLDL (C) IDL (D) HDL 237. A lipoprotein inversely related to the incidence of coronary arthrosclerosis is  (A) VLDL (B) IDL (C) LDL (D) HDL 238. The primary biochemical lesion in homozygote with familial hypercholesterolemia (type IIa) is (A) Loss of feedback inhibition of HMG reductase (B) Loss of apo lipoprotein B (C) Increased production of LDL from VLDL (D) Functional deficiency of plasma membrane receptors for LDL 239. In abetalipoproteinemia, the biochemical defect is in (A) Apo-B synthesis (B) Lipprotein lipase activity (C) Cholesterol ester hydrolase (D) LCAT activity 240. Familial hyper triacylglycerolemia is associated with (A) Over production of VLDL (B) Increased LDL concentration (C) Increased HDL concentration (D) Slow clearance of chylomicrons 241. For synthesis of prostaglandins, the essential fatty acids give rise to a fatty acid containing (A) 12 carbon atoms (B) 16 carbon atoms (C) 20 carbon atoms (D) 24 carbon atoms 242. All active prostaglandins have at least one double bond between positions (A) 7 and 8 (B) 10 and 11 (C) 13 and 14 (D) 16 and 17 243. Normal range of plasma total phospholipids is (A) 0.2–0.6 mmol/L (B) 0.9–2.0 mmol/L (C) 1.8–5.8 mmol/L (D) 2.8–5.3 mmol/L 244. HDL2 have the density in the range of (A) 1.006–1.019 (B) 1.019–1.032 (C) 1.032–1.063 (D) 1.063–1.125 245. β-lipoproteins have the density in the range of (A) 0.95–1.006 (B) 1.006–1.019 (C) 1.019–1.063 (D) 1.063–1.125 246. IDL have the density in the range of (A) 0.95–1.006 (B) 1.006–1.019 (C) 1.019–1.032 (D) 1.032–1.163 247. Aspirin inhibits the activity of the enzyme: (A) Lipoxygenase (B) Cyclooxygenase (C) Phospholipae A1 (D) Phospholipase A2 248. A ’suicide enzyme’ is (A) Cycloxygenase (B) Lipooxygenase (C) Phospholipase A1 (D) Phospholipase A2 249. In adipose tissue prostaglandins decrease (A) (A)Lipogenesis (B) Lipolysis (C) Gluconeogenesis (D) Glycogenolysis 250. The optimal pH for the enzyme pepsin is (A) 1.0–2.0 (B) 4.0–5.0 (C) 5.2– 6.0 (D) 5.8–6.2 251. Pepsinogen is converted to active pepsin by (A) HCl (B) Bile salts (C) Ca ++ (D) Enterokinase 252. The optimal pH for the enzyme rennin is (A) 2.0 (B) 4.0 (C) 8.0  (D) 6.0 253. The optimal pH for the enzyme trypsin is (A) 1.0–2.0 (B) 2.0–4.0 (C) 5.2–6.2 (D) 5.8–6.2 254. The optimal pH for the enzyme chymotrypsin is (A) 2.0 (B) 4.0 (C) 6.0 (D) 8.0 255. Trypsinogen is converted to active trypsin by (A) Enterokinase (B) Bile salts (C) HCl (D) Mg ++ 256. Pepsin acts on denatured proteins to produce (A) Proteoses and peptones (B) Polypeptides (C) Peptides (D) Dipeptides 257. Renin converts casein to paracasein in presence of (A) Ca++ (B) Mg++ (C) Na+ (D) K+ 258. An expopeptidase is (A) Trypsin (B) Chymotrypsin (C) Elastase (D) Elastase 259. The enzyme trypsin is specific for peptide bonds of (A) Basic amino acids (B) Acidic amino acids (C) Aromatic amino acids (D) Next to small amino acid residues 260. Chymotrypsin is specific for peptide bonds containing (A) Uncharged amino acid residues  (B) Acidic amino acids (C) Basic amino acid (D) Small amino acid residues 261. The end product of protein digestion in G.I.T. is (A) Dipeptide (B) Tripeptide (C) Polypeptide (D) Amino acid 262. Natural L-isomers of amino acids are absorbed from intestine by (A) Passive diffusion (B) Simple diffusion (C) Faciliated diffusion (D) Active process 263. Abnormalities of blood clotting are (A) Haemophilia (B) Christmas disease (C) Gout (D) Both (A) and (B) 264. An important reaction for the synthesis of amino acid from carbohydrate intermediates is transamination which requires the cofactor: (A) Thiamin (B) Riboflavin (C) Niacin (D) Pyridoxal phosphate 265. Which among the following is an essential amino acid? (A) Cysteine (B) Leucine (C) Tyrosine (D) Aspartic acid 266. Which among the following is a basic amino acid? (A) Aspargine (B) Arginine (C) Proline (D) Alanine 267. This amino acid cannot have optical isomers: (A) Alanine (B) Histidine (C) Threonine (D) Glycine 268. The amino acid which contains a guanidine group is (A) Histidine (B) Arginine (C) Citrulline (D) Ornithine 269. GABA (gama amino butyric acid) is (A) Post-synaptic excitatory transmitter (B) Post-synaptic inhibitor transmitter (C) activator of glia-cell function (D) inhibitor of glia-cell function 270. Sulphur-containing amino acid is (A) Glutathione (B) Chondroitin sulphate (C) Homocysteine (D) Tryptophan 271. The useful reagent for detection of amino acids is (A) Molisch reagent (B) Dichlorophenol Indophenol (C) Ninhydrin (D) Biuret 272. The amino acid which contains an indole group is (A) Histidine (B) Arginine (C) Glycine (D) Tryptophan 273. The major end product of protein nitrogen metabolism in man is (A) Glycine (B) Uric acid (C) Urea (D) NH3 274. An amino acid not involved in urea cycle is (A) Arginine (B) Histidine (C) Ornithine (D) Citrulline 275. NH3 is detoxified in brain chiefly as (A) Urea (B) Uric acid (C) Creatinine  (D) Glutamine 276. In humans, NH3 is detoxified in liver as (A) Creatinine (B) Uric acid (C) Urea (D) Uronic acid 277. The body protein after eighteen years (A) Remains unchanged (B) Is decomposed only slightly at intervals of one month (C) Is in a constant state of flux (D) Is used only for energy requirement 278. The only known physiological methylating agents in the animal organism are (A) Choline and betaine (B) Choline and δ-adenosyl methionine (C) Betaine and δ -adenyosyl methionine (D) Dimehtyl glycine and betaine 279. Ammonia production by the kidney is depressed in (A) Acidosis (B) Alkalosis (C) Both (A) and (B) (D) None of these 280. Ammonia is excreted as ammonium salts during metabolic acidosis but the majority is excreted as (A) Phosphates (B) Creatine (C) Uric acid (D) Urea 281. Synthesis of glutamine is accompanied by the hydrolysis of (A) ATP (B) ADP (C) TPP (D) Creatin phosphate 282. In brain, the major metabolism for removal of ammonia is the formation of (A) Glutamate (B) Aspartate (C) Asparagine (D) Glutamine 283. Carbamoyl phosphate synthetase structure is marked by change in the presence of (A) N-Acetyl glutamate (B) N-Acetyl Aspartate  (C) Neuraminic acid (D) Oxalate 284. The biosynthesis of Urea occurs mainly in the Liver: (A) Cytosol (B) Microsomes (C) Nucleus (D) Mitochondria 285. One mol. of Urea is synthesized at the expense of the _______ mols. of ATP. (A) 2 (B) 3 (C) 4 (D) 5 286. Urea biosynthesis occurs mainly in the liver involving the number of amino acids: (A) 3 (B) 4 (C) 5 (D) 6 287. The normal daily output of Urea through urine in grams: (A) 10 to 20 (B) 15 to 25 (C) 20 to 30 (D) 25 to 35 288. In severe acidosis, the output of urea is (A) Decreased (B) Slightly increased (C) Highly increased (D) Moderately increased 289. Uremia occurs in (A) Cirrhosis of the liver (B) Nephritis (C) Diabetes mellitus (D) Coronary thrombosis 290. Clinical symptom in urea cycle disorder is (A) Mental retardation (B) Drowsiness (C) Diarrhea (D) Oedema 291. The sparing action of methionine is (A) Tyrosine  (B) Cystine (C) Arginine (D) Tryptophan 292. NH+4 aminates glutamate to form glutamine requiring ATP and (A) K+ (B) Na+ (C) Ca++ (D) Mg++ 293. Glutathione is a (A) Dipeptide (B) Tripeptide (C) Polypeptide (D) None of these 294. All following are conjugated proteins except (A) Nucleoproteins (B) Proteoses (C) Metalloproteins (D) Flavoproteins 295. All α-amino acids have one asymmetric carbon atom except (A) Arginine (B) Glycine (C) Aspartic acid (D) Histidine 296. Number of amino acids present in plants, animals and microbial proteins: (A) 20 (B) 80 (C) 150 (D) 200 297. Hydrated density of (HD) lipoproteins is (A) 0.94 gm/ml (B) 0.94-1.006 gm/ml (C) 1.006-1.063 gm/ml (D) 1.063-1.21 gm/l 298. The bond in proteins that is not broken under usual conditions of denaturation: (A) Hydrophobic bond (B) Hydrogen bond (C) Disulphide bond (D) Peptide bonds 299. 632. Plasma proteins act as  (A) Buffers (B) Immunoglobulins (C) Reserve proteins (D) All of these 300. Group that reacts in the Biuret test: (A) Peptide (B) Amino group (C) Carboxylic group (D) Aldehyde group 301. In nitroprusside test, amino acid cysteine produces a: (A) Red color (B) Blue color (C) Yellow color (D) Purple color 302. Protein present in hemoglobin has the structure known as (A) Primary (B) Secondary (C) Tertiary (D) Quarternary 303. Isoelectric pH of an amino acid is that pH at which it has a (A) Positive charge (B) Negative charge (C) Nil net charge (D) None of these 304. Albuminoids are similar to (A) Albumin (B) Globulin (C) Both (A) and (B) (D) None of these 305. Optical isomers of all amino acids exist except (A) Glycine (B) Arginine (C) Alanine (D) Hydroxy proline 306. Proteins that constitute keratin, collagen and elastin in body are (A) Protamines (B) Phosphol proteins (C) Scleroproteins (D) Metaproteins 307. Systematic name of lysine is (A) Amino acetic acid (B) 2,6 diaminohexanoic acid (C) Aminosuccinic acid (D) 2-Aminopropanoic acid 308. Side chains of all following amino acids contain aromatic rings except (A) Phenyl alanine (B) Alanine (C) Tyrosine (D) Tryptophan 309. Abnormal chain of amino acids in sickle cell anaemia is (A) Alpha chain (B) Beta chain (C) Delta chain (D) Gama chain 310. Number of chains in globin part of normal Hb: (A) 1 (B) 2 (C) 3 (D) 4 311. The PH of albumin is (A) 3.6 (B) 4.7 (C) 5.0 (D) 6.1 312. Ninhydrin reaction gives a purple color and evolves CO2 with (A) Peptide bonds (B) Histamine (C) Ergothioneine (D) Aspargine 313. Denaturation of proteins involves breakdown of (A) Secondary structure (B) Tertiary structure (C) Quarternary structure (D) All of these 314. In denaturation of proteins, the bond which is not broken: (A) Disulphide bond (B) Peptide bond (C) Hydrogen bond  (D) Ionic bond 315. The purity of an isolated protein can be tested by employing various methods. (A) Solubility curve (B) Molecular weight (C) Ultra Centrifugation (D) Immuno Ractivity (E) All of these 316. More than one break in the line or in saturation curve indicates the following quality of protein. (A) Non homogenity (B) Purity (C) Homogeneity (D) None of these 317. A sharp moving boundary is obtained between the pure solvent and solute containing layer in (A) Chromatography (B) Immuno Reactivity (C) Ultra Centrifugation (D) Solubility curve 318. An example of a hydroxy fatty acid is (A) Ricinoleic acid (B) Crotonic acid (C) Butyric acid (D) Oleic acid 319. An example of a saturated fatty acid is (A) Palmitic acid (B) Oleic acid (C) Linoleic acid (D) Erucic acid 320. If the fatty acid is esterified with an alcohol of high molecular weight instead of glycerol, the resulting compound is (A) Lipositol (B) Plasmalogen (C) Wax (D) Cephalin 321. A fatty acid which is not synthesized in the body and has to be supplied in the diet is (A) Palmitic acid (B) Lauric acid (C) Linolenic acid (D) Palmitoleic acid 322. Essential fatty acid:  (A) Linoleic acid (B) Linolenic acid (C) Arachidonic acid (D) All these 323. The fatty acid present in cerebrosides is (A) Lignoceric acid (B) Valeric acid (C) Caprylic acid (D) Behenic acid 324. The number of double bonds in arachidonic acid is (A) 1 (B) 2 (C) 4 (D) 6 325. In humans, a dietary essential fatty acid is (A) Palmitic acid (B) Stearic acid (C) Oleic acid (D) Linoleic acid 326. A lipid containing alcoholic amine residue is (A) Phosphatidic acid (B) Ganglioside (C) Glucocerebroside (D) Sphingomyelin 327. Cephalin consists of (A) Glycerol, fatty acids, phosphoric acid and choline (B) Glycerol, fatty acids, phosphoric acid and ethanolamine (C) Glycerol, fatty acids, phosphoric acid and inositol (D) Glycerol, fatty acids, phosphoric acid and serine 328. In mammals, the major fat in adipose tissues is (A) Phospholipid (B) Cholesterol (C) Sphingolipids (D) Triacylglycerol 329. Glycosphingolipids are a combination of (A) Ceramide with one or more sugar residues (B) Glycerol with galactose (C) Sphingosine with galactose (D) Sphingosine with phosphoric acid 330. The importance of phospholipids as constituent of cell membrane is because they possess (A) Fatty acids (B) Both polar and nonpolar groups (C) Glycerol (D) Phosphoric acid 331. In neutral fats, the un saponificable matter includes (A) Hydrocarbons (B) Triacylglycerol (C) Phospholipids (D) Cholsesterol 332. Higher alcohol present in waxes is (A) Benzyl (B) Methyl (C) Ethyl (D) Cetyl 333. Kerasin consists of (A) Nervonic acid (B) Lignoceric acid (C) Cervonic acid (D) Clupanodonic acid 334. Gangliosides are complex glycosphingolipids found in (A) Liver (B) Brain (C) Kidney (D) Muscle 335. Unsaturated fatty acid found in the cod liver oil and containing 5 double bonds is (A) Clupanodonic acid (B) Cervonic acid (C) Elaidic acid (D) Timnodonic acid 336. Phospholipid acting as surfactant is (A) Cephalin (B) Phosphatidyl inositol (C) Lecithin (D) Phosphatidyl serine 337. An oil which contains cyclic fatty acids and once used in the treatment of leprosy is (A) Elaidic oil (B) Rapeseed oil (C) Lanoline  (D) Chaulmoogric oil 338. Unpleasant odours and taste in a fat (rancidity) can be delayed or prevented by the addition of (A) Lead (B) Copper (C) Tocopherol (D) Ergosterol 339. Gangliosides derived from glucosylceramide contain in addition one or more molecules of (A) Sialic acid (B) Glycerol (C) Diacylglycerol (D) Hyaluronic acid 340. ’Drying oil’, oxidized spontaneously by atmospheric oxygen at ordinary temperature and forms a hard water proof material is (A) Coconut oil (B) Peanut oil (C) Rape seed oil (D) Linseed oil 341. Deterioration of food (rancidity) is due to presence of (A) Cholesterol (B) Vitamin E (C) Peroxidation of lipids (D) Phenolic compounds 342. The number of ml of N/10 KOH required to neutralize the fatty acids in the distillate from 5 gm of fat is called (A) Reichert-Meissel number (B) Polenske number (C) Acetyl number (D) Non volatile fatty acid number 343. Molecular formula of cholesterol is (A) C27H45OH (B) C29H47OH (C) C29H47OH (D) C23H41OH 344. The cholesterol molecule is (A) Benzene derivative (B) Quinoline derivative (C) Steroid (D) Straight chain acid 345. Salkowski test is performed to detect  (A) Glycerol (B) Cholesterol (C) Fatty acids (D) Vitamin D 346. Palmitic, oleic or stearic acid ester of cholesterol used in manufacture of cosmetic creams is (A) Elaidic oil (B) Lanoline (C) Spermaceti (D) Chaulmoogric oil 347. Dietary fats after absorption appear in the circulation as (A) HDL (B) VLDL (C) LDL (D) Chylomicron 348. Free fatty acids are transported in the blood (A) Combined with albumin (B) Combined with fatty acid binding protein (C) Combined with beta lipoprotein (D) In unbound free salts 349. Long chain fatty acids are first activated to acetyl-CoA in (A) Cytosol (B) Microsomes (C) Nucleus (D) Mitochondria 350. The enzyme acyl-CoA synthase catalyses the conversion of a fatty acid of an active fatty acid in the presence of (A) AMP (B) ADP (C) ATP (D) GTP 351. Carnitine is synthesized from (A) Lysine and methionine (B) Glycine and arginine (C) Aspartate and glutamate (D) Proline and hydroxyproline 352. The enzymes of beta-oxidation are found in (A) Mitochondria (B) Cytosol (C) Golgi apparatus  (D) Nucleus 353. Long chain fatty acids penetrate the inner mitochondrial membrane (A) Freely (B) As acyl-CoA derivative (C) As carnitine derivative (D) Requiring Na dependent carrier 354. An important feature of Zellweger’s syndrome is (A) Hypoglycemia (B) Accumulation of phytanic acid in tissues (C) Skin eruptions (D) Accumulation of C26-C38 polyenoic acid in brain tissues 355. An important finding of Fabry’s disease is (A) Skin rash (B) Exophthalmos (C) Hemolytic anemia (D) Mental retardation 356. Gaucher’s disease is due to deficiency of the enzyme: (A) Sphingomyelinase (B) Glucocerebrosidase (C) Galactocerbrosidase (D) beta-Galactosidase 357. Characteristic finding in Gaucher’s disease is (A) Night blindness (B) Renal failure (C) Hepatosplenomegaly (D) Deafness 358. An important finding in Neimann-Pick disease is (A) Leukopenia (B) Cardiac enlargement (C) Corneal opacity (D) Hepatosplenomegaly 359. Fucosidosis is characterized by (A) Muscle spasticity (B) Liver enlargement (C) Skin rash (D) Kidney failure 360. Metachromatic leukodystrophy is due to deficiency of enzyme: (A) alpha-Fucosidase (B) Arylsulphatase A  (C) Ceramidase (D) Hexosaminidase A 361. A significant feature of Tangier disease is (A) Impairment of chylomicron formation (B) Hypotriacylglycerolmia (C) Absence of Apo-C-II (D) Absence of Apo-C-I 362. A significant feature of Broad Beta disease is (A) Hypocholesterolemia (B) Hypotriacylglycerolemia (C) Absence of Apo-D (D) Abnormality of Apo-E 363. Neonatal tyrosinemia improves on administration of (A) Thiamin (B) Riboflavin (C) Pyridoxine (D) Ascorbic acid 364. Absence of phenylalanine hydroxylase causes (A) Neonatal tyrosinemia (B) Phenylketonuria (C) Primary hyperoxaluria (D) Albinism 365. Richner-Hanhart syndrome is due to defect in (A) Tyrosinase (B) Phenylalanine hydroxylase (C) Hepatic tyrosine transaminase (D) Fumarylacetoacetate hydrolase 366. Plasma tyrosine level in Richner-Hanhart syndrome is (A) 1–2 mg/dL (B) 2–3 mg/dL (C) 4–5 mg/dL (D) 8–10 mg/dL 367. Amount of phenylacetic acid excreted in the urine in phenylketonuria is (A) 100–200 mg/dL (B) 200–280 mg/dL (C) 290–550 mg/dL (D) 600–750 mg/dL 368. Tyrosinosis is due to defect in the enzyme: (A) Fumarylacetoacetate hydrolase  (B) p-Hydroxyphenylpyruvate hydroxylase (C) Tyrosine transaminase (D) Tyrosine hydroxylase 369. An important finding in Histidinemia is (A) Impairment of conversion of alpha-Glutamate to alpha-ketoglutarate (B) Speech defect (C) Decreased urinary histidine level (D) Patients can not be treated by diet 370. An important finding in glycinuria is (A) Excess excretion of oxalate in the urine (B) Deficiency of enzyme glycinase (C) Significantly increased serum glycine level (D) Defect in renal tubular reabsorption of glycine 371. Increased urinary indole acetic acid is diagnostic of (A) Maple syrup urine disease (B) Hartnup disease (C) Homocystinuia (D) Phenylketonuria 372. In glycinuria daily urinary excretion of glycine ranges from (A) 100–200 mg (B) 300–500 mg (C) 600–1000 mg (D) 1100–1400 mg 373. An inborn error, maple syrup urine disease is due to deficiency of the enzyme: (A) Isovaleryl-CoAhydrogenase (B) Phenylalnine hydroxylase (C) Adenosyl transferase (D) alpha-Ketoacid decarboxylase 374. Maple syrup urine disease becomes evident in extra uterine life by the end of (A) First week (B) Second week (C) Third week (D) Fourth week 375. Alkaptonuria occurs due to deficiency of the enzyme: (A) Maleylacetoacetate isomerase (B) Homogentisate oxidase (C) p-Hydroxyphenylpyruvate hydroxylase (D) Fumarylacetoacetate hydrolase 376. An important feature of maple syrup urine disease is  (A) Patient cannot be treated by dietary regulation (B) Without treatment death, of patient may occur by the end of second year of life (C) Blood levels of leucine, isoleucine and serine are increased (D) Excessive brain damage 377. Ochronosis is an important finding of (A) Tyrosinemia (B) Tyrosinosis (C) Alkaptonuria (D) Richner Hanhart syndrome 378. Phrynoderma is a deficiency of (A) Essential fatty acids (B) Proteins (C) Amino acids (D) None of these 379. The percentage of linoleic acid in safflower oil is (A) 73 (B) 57 (C) 40 (D) 15 380. The percentage of polyunsaturated fatty acids in soyabean oil is (A) 62 (B) 10 (C) 3 (D) 2 381. The percentage of polyunsaturated fatty acids in butter is (A) 60 (B) 37 (C) 25 (D) 3 382. Dietary fiber denotes (A) Undigested proteins (B) Plant cell components that cannot be digested by own enzymes (C) All plant cell wall components (D) All non-digestible water insoluble polysaccharide 383. A high fiber diet is associated with reduced incidence of (A) Cardiovascular disease (B) C.N.S. disease (C) Liver disease (D) Skin disease 384. Dietary fibers are rich in (A) Cellulose (B) Glycogen (C) Starch (D) Proteoglycans 385. Minimum dietary fiber is found in (A) Dried apricot (B) Peas (C) Bran (D) Cornflakes 386. A bland diet is recommended in (A) Peptic ulcer (B) Atherosclerosis (C) Diabetes (D) Liver disease 387. A dietary deficiency in both the quantity and the quality of protein results in (A) Kwashiorkar (B) Marasmus (C) Xerophtalmia (D) Liver diseases 388. The deficiency of both energy and protein causes (A) Marasmus (B) Kwashiorkar (C) Diabetes (D) Beri-beri 389. Kwashiorkar is characterized by (A) Night blindness (B) Edema (C) Easy fracturability (D) Xerophthalmia 390. A characteristic feature of Kwashiorkar is (A) Fatty liver (B) Emaciation (C) Low insulin lever (D) Occurrence in less than 1 year infant 391. A characteristic feature of marasmus is (A) Severe hypoalbuminemia (B) Normal epinephrine level (C) Mild muscle wasting  (D) Low insulin and high cortisol level 392. Obesity generally reflects excess intake of energy and is often associated with the development of (A) Nervousness (B) Non-insulin dependent diabetes mellitus (C) Hepatitis (D) Colon cancer 393. Atherosclerosis and coronary heart diseases are associated with the diet: (A) High in total fat and saturated fat (B) Low in protein (C) High in protein (D) High in carbohydrate 394. Cerebrovasular disease and hypertension is associated with (A) High calcium intake (B) High salt intake (C) Low calcium intake (D) Low salt intake 395. The normal range of total serum bilirubin is (A) 0.2–1.2 mg/100 ml (B) 1.5–1.8 mg/100 ml (C) 2.0–4.0 mg/100 ml (D) Above 7.0 mg/100 ml 396. The normal range of direct reacting (conjugated) serum bilirubin is (A) 0–0.1 mg/100 ml (B) 0.1–0.4 mg/100 ml (C) 0.4–06 mg/100 ml (D) 0.5–1 mg/100 ml 397. The normal range of indirect (unconjugated) bilirubin in serum is (A) 0–0.1 mg/100 ml (B) 0.1–0.2 mg/100 ml (C) 0.2–0.7 mg/100 ml (D) 0.8–1.0 mg/100 ml 398. Jaundice is visible when serum bilirubin exceeds (A) 0.5 mg/100 ml (B) 0.8 mg/100 ml (C) 1 mg/100 ml (D) 2.4 mg/100 ml 399. An increase in serum unconjugated bilirubin occurs in (A) Hemolytic jaundice (B) Obstructive jaundice  (C) Nephritis (D) Glomerulonephritis 400. One of the causes of hemolytic jaundice is (A) G-6 phosphatase deficiency (B) Increased conjugated bilirubin (C) Glucokinase deficiency (D) Phosphoglucomutase deficiency 401. Increased urobilinogen in urine and absence of bilirubin in the urine suggests (A) Obstructive jaundice (B) Hemolytic jaundice (C) Viral hepatitis (D) Toxic jaundice 402. A jaundice in which serum alanine transaminase and alkaline phosphatase are normal is (A) Hepatic jaundice (B) Hemolytic jaundice (C) Parenchymatous jaundice (D) Obstructive Jaundice 403. Fecal stercobilinogen is increased in (A) Hemolytic jaundice (B) Hepatic jaundice (C) Viral hepatitis (D) Obstructive jaundice 404. Fecal urobilinogen is increased in (A) Hemolytic jaundice (B) Obstruction of biliary duct (C) Extrahepatic gall stones (D) Enlarged lymphnodes 405. A mixture of conjugated and unconjugated bilirubin is found in the circulation in (A) Hemolytic jaundice (B) Hepatic jaundice (C) Obstructive jaundice (D) Post hepatic jaundice 406. Hepatocellular jaundice as compared to pure obstructive type of jaundice is characterized by (A) Increased serum alkaline phosphate, LDH and ALT (B) Decreased serum alkaline phosphatase, LDH and ALT (C) Increased serum alkaline phosphatase and decreased levels of LDH and ALT (D) Decreased serum alkaline phosphatase and increased serum LDH and ALT 407. Icteric index of an normal adult varies between (A) 1–2  (B) 2–4 (C) 4–6 (D) 10–15 408. Clinical jaundice is present with an icteric index above (A) 4 (B) 8 (C) 10 (D) 15 409. Normal quantity of urobilinogen excreted in the feces per day is about (A) 10–25 mg (B) 50–250 mg (C) 300–500 mg (D) 700–800 mg 410. Fecal urobilinogen is decreased in (A) Obstruction of biliary duct (B) Hemolytic jaundice (C) Excess fat intake (D) Low fat intake 411. A complete absence of fecal urobilinogen is strongly suggestive of (A) Obstruction of bile duct (B) Hemolytic jaundice (C) Intrahepatic cholestasis (D) Malignant obstructive disease 412. Immediate direct Vanden Bergh reaction indicates (A) Hemolytic jaundice (B) Hepatic jaundice (C) Obstructive jaundice (D) Megalobastic anemia 413. The presence of bilirubin in the urine without urobilinogen suggests (A) Obstructive jaundice (B) Hemolytic jaundice (C) Pernicious anemia (D) Damage to the hepatic parenchyma 414. Impaired galactose tolerance test suggests (A) Defect in glucose utilisation (B) Liver cell injury (C) Renal defect (D) Muscle injury 415. Increased serum ornithine carabamoyl transferase activity is diagnostic of  (A) Myocardial infarction (B) Hemolytic jaundice (C) Bone disease (D) Acute viral hepatitis 416. The best known and most frequently used test of the detoxicating functions of liver is (A) Hippuric acid test (B) Galactose tolerance test (C) Epinephrine tolerance test (D) Rose Bengal dye test 417. The ability of liver to remove a dye like BSP from the blood suggests a normal (A) Excretory function (B) Detoxification function (C) Metabolic function (D) Circulatory function 418. Removal of BSP dye by the liver involves conjugation with (A) Thiosulphate (B) Glutamine (C) Cystein component of glutathione (D) UDP glucuronate 419. Normal value of plasma total proteins varies between (A) 3–4 gm/100ml (B) 6–8 gm/100ml (C) 10–12 gm/100ml (D) 14–16 gm/100ml 420. A decrease in albumin with increased production of other unidentified proteins which migrate in beta, gema region suggests (A) Cirrhosis of liver (B) Nephrotic syndrome (C) Infection (D) Chronic lymphatic leukemia 421. In increase in α2-Globulin with loss of albumin in urine suggests (A) Primary immune deficiency (B) Nephrotic syndrome (C) Cirrhosis of liver (D) Multiple myeloma 422. Vitamins are (A) Accessory food factors (B) Generally synthesized in the body (C) Produced in endocrine glands  (D) Proteins in nature 423. Vitamin A or retinal is a (A) Steroid (B) Polyisoprenoid compound containing a cyclohexenyl ring (C) Benzoquinone derivative (D) 6-Hydroxychromane 424. beta-Carotene, precursor of vitamin A, is oxidatively cleaved by (A) beta-Carotene dioxygenase (B) Oxygenase (C) Hydroxylase (D) Transferase 425. Retinal is reduced to retinol in intestinal mucosa by a specific retinaldehyde reductase utilizing (A) NADPH + H + (B) FAD (C) NAD (D) NADH + H+ 426. Preformed Vitamin A is supplied by (A) Milk, fat and liver (B) All yellow vegetables (C) All yellow fruits (D) Leafy green vegetables 427. Retinol and retinal are interconverted requiring dehydrogenase or reductase in the presence of (A) NAD or NADP (B) NADH + H+ (C) NADPH (D) FAD 428. Fat soluble vitamins are (A) Soluble in alcohol (B) one or more Propene units (C) Stored in liver (D) All these 429. The international unit of vitamin A is equivalent to the activity caused by (A) 0.3 µg of Vitamin A alcohol (B) 0.344 µg of Vitamin A alcohol (C) 0.6 µg of Vitamin A alcohol (D) 1.0 µg of Vitamin A alcohol 430. Lumirhodopsin is stable only at temperature below (A) –10°C (B) –20°C  (C) –40°C (D) –50°C 431. Retinol is transported in blood bound to (A) Aporetinol binding protein (B) α2-Globulin (C) beta-Globulin (D) Albumin 432. The normal serum concentration of vitamin A in mg/100 ml is (A) 5–10 (B) 15–60 (C) 100–150 (D) 0–5 433. One manifestation of vitamin A deficiency is (A) Painful joints (B) Night blindness (C) Loss of hair (D) Thickening of long bones 434. Deficiency of Vitamin A causes (A) Xeropthalmia (B) Hypoprothrombinemia (C) Megaloblastic anemia (D) Pernicious anemia 435. An important function of vitamin A is (A) To act as coenzyme for a few enzymes (B) To play an integral role in protein synthesis (C) To prevent hemorrhages (D) To maintain the integrity of epithelial tissue 436. Retinal is a component of (A) Iodopsin (B) Rhodopsin (C) Cardiolipin (D) Glycoproteins 437. Retinoic acid participates in the synthesis of (A) Iodopsin (B) Rhodopsin (C) Glycoprotein (D) Cardiolipin 438. On exposure to light rhodopsin forms (A) All trans-retinal  (B) Cis-retinal (C) Retinol (D) Retinoic acid 439. Carr-Price reaction is used to detect (A) Vitamin A (B) Vitamin D (C) Ascorbic acid (D) Vitamin E 440. The structure shown below is of (A) Cholecalciferol (B) 25-Hydroxycholecalciferol (C) Ergocalciferol (D) 7-Dehydrocholesterol 441. Vitamin D absorption is increased in (A) Acid pH of intestine (B) Alkaline pH of intestine (C) Impaired fat absorption (D) Contents of diet 442. The most potent Vitamin D metabolite is (A) 25-Hydroxycholecalciferol (B) 1,25-Dihydroxycholecalciferol (C) 24, 25-Dihydroxycholecalciferol (D) 7-Dehydrocholesterol 443. The normal serum concentration of 25-hydroxycholecalciferol in ng/ml is (A) 0–8 (B) 60–100 (C) 100–150 (D) 8–55 444. The normal serum concentration of 1,25-dihydroxycholecalciferol in pg/ml is (A) 26–65 (B) 1–5 (C) 5–20 (D) 80–100 445. The normal serum concentration of 24,25- dihydroxycholecalciferol in ng/ml is (A) 8–20 (B) 25–50 (C) 1–5 (D) 60–100 446. A poor source of Vitamin D is  (A) Egg (B) Butter (C) Milk (D) Liver 447. Richest source of Vitamin D is (A) Fish liver oils (B) Margarine (C) Egg yolk (D) Butter 448. Deficiency of vitamin D causes (A) Ricket and osteomalacia (B) Tuberculosis of bone (C) Hypthyroidism (D) Skin cancer 449. One international unit (I.U) of vitamin D is defined as the biological activity of (A) 0.025 µg of cholecalciferol (B) 0.025 µg of 7-dehydrocholecalciferol (C) 0.025 µg of ergosterol (D) 0.025 µg of ergocalciferol 450. The beta-ring of 7-dehydrocholesterol is cleaved to form cholecalciferol by (A) Infrared light (B) Dim light (C) Ultraviolet irridation with sunlight (D) Light of the tube lights 451. Calcitriol synthesis involves (A) Both liver and kidney (B) Intestine (C) Adipose tissue (D) Muscle 452. Insignificant amount of Vitamin E is present in (A) Wheat germ oil (B) Sunflower seed oil (C) Safflower seed oil (D) Fish liver oil 453. The activity of tocopherols is destroyed by (A) Commercial cooking (B) Reduction (C) Conjugation (D) All of these 454. The requirement of vitamin E is increased with greater intake of (A) Carbohydrates (B) Proteins (C) Polyunsaturated fat (D) Saturated fat 455. Vitamin E reduces the requirement of (A) Iron (B) Zinc (C) Selenium (D) Magnesium 456. The most important natural antioxidant is (A) Vitamin D (B) Vitamin E (C) Vitamin B12 (D) Vitamin K 457. Tocopherols prevent the oxidation of (A) Vitamin A (B) Vitamin D (C) Vitamin K (D) Vitamin C 458. Creatinuria is caused due to the deficiency of vitamin (A) A (B) K (C) E (D) D 459. All the following conditions produce a real or functional deficiency of vitamin K except (A) Prolonged oral, broad spectrum antibiotic therapy (B) Total lack of red meat in the diet (C) The total lack of green leafy vegetables in the diet (D) Being a new born infant 460. Vitamin K is found in (A) Green leafy plants (B) Meat (C) Fish (D) Milk 461. Function of Vitamin A: (A) Healing epithelial tissues (B) Protein synthesis regulation (C) Cell growth  (D) All of these 462. Vitamin K2 was originally isolated from (A) Soyabean (B) Wheat gram (C) Alfa Alfa (D) Putrid fish meal 463. Vitamin synthesized by bacterial in the intestine is (A) A (B) C (C) D (D) K 464. Vitamin K is involved in posttranslational modification of the blood clotting factors by acting as cofactor for the enzyme: (A) Carboxylase (B) Decarboxylase (C) Hydroxylase (D) Oxidase 465. Vitamin K is a cofactor for (A) Gamma carboxylation of glutamic acid residue (B) beta-Oxidation of fatty acid (C) Formation of γ-amino butyrate (D) Synthesis of tryptophan 466. Hypervitaminosis K in neonates may cause (A) Porphyria (B) Jaundice (C) Pellagra (D) Prolonged bleeding 467. Dicoumarol is antagonist to (A) Riboflavin (B) Retinol (C) Menadione (D) Tocopherol 468. In the individuals who are given liberal quantities of vitamin C, the serum ascorbic acid level is (A) 1–1.4 μg/100 ml (B) 2–4 μg/100 ml (C) 1–10 μg/100 ml (D) 10–20 μg/100 ml 469. The vitamin which would most likely become deficient in an individual who develop a completely carnivorous life style is  (A) Thiamin (B) Niacin (C) Vitamin C (D) Cobalamin 470. In human body highest concentration of ascorbic acid is found in (A) Liver (B) Adrenal cortex (C) Adrenal medulla (D) Spleen 471. The vitamin required for the formation of hydroxyproline (in collagen) is (A) Vitamin C (B) Vitamin A (C) Vitamin D (D) Vitamin E 472. Vitamin required for the conversion of p-hydroxyphenylpyruvate to homogentisate is (A) Folacin (B) Cobalamin (C) Ascorbic acid (D) Niacin 473. Vitamin required in conversion of folic acid to folinic acid is (A) Biotin (B) Cobalamin (C) Ascorbic acid (D) Niacin 474. Ascorbic acid can reduce (A) 2, 6-Dibromobenzene (B) 2, 6-Diiodoxypyridine (C) 2, 6-Dichlorophenol indophenol (D) 2, 4-Dinitrobenzene 475. Sterilised milk lacks in (A) Vitamin A (B) Vitamin D (C) Vitamin C (D) Thiamin 476. Scurvy is caused due to the deficiency of (A) Vitamin A (B) Vitamin D (C) Vitamin K (D) Vitamin C 477. Both Wernicke’s disease and beriberi can be reversed by administrating (A) Retinol (B) Thiamin (C) Pyridoxine (D) Vitamin B12 478. The Vitamin B1 deficiency causes (A) Ricket (B) Nyctalopia (C) Beriberi (D) Pellagra 479. Concentration of pyruvic acid and lactic acid in blood is increased due to deficiency of the vitamin (A) Thiamin (B) Riboflavin (C) Niacin (D) Pantothenic acid 480. Vitamin B1 coenzyme (TPP) is involved in (A) Oxidative decarboxylation (B) Hydroxylation (C) Transamination (D) Carboxylation 481. Increased glucose consumption increases the dietary requirement for (A) Pyridoxine (B) Niacin (C) Biotin (D) Thiamin 482. Thiamin is oxidized to thiochrome in alkaline solution by (A) Potassium permanganate (B) Potassium ferricyanide (C) Potassium chlorate (D) Potassium dichromate 483. Riboflavin is a coenzyme in the reaction catalysed by the enzyme (A) Acyl CoA synthetase (B) Acyl CoA dehydrogenase (C) beta-Hydroxy acyl CoA (D) Enoyl CoA dehydrogenase 484. The daily requirement of riboflavin for adult in mg is (A) 0–1.0 (B) 1.2–1.7  (C) 2.0–3.5 (D) 4.0–8.0 485. In new born infants phototherapy may cause hyperbilirubinemia with deficiency of (A) Thiamin (B) Riboflavin (C) Ascorbic acid (D) Pantothenic acid 486. Riboflavin deficiency causes (A) Cheilosis (B) Loss of weight (C) Mental deterioration (D) Dermatitis 487. Magenta tongue is found in the deficiency of the vitamin (A) Riboflavin (B) Thiamin (C) Nicotinic acid (D) Pyridoxine 488. Corneal vascularisation is found in deficiency of the vitamin: (A) B1 (B) B2 (C) B3 (D) B6 489. The pellagra preventive factor is (A) Riboflavin (B) Pantothenic acid (C) Niacin (D) Pyridoxine 490. Pellagra is caused due to the deficiency of (A) Ascorbic acid (B) Pantothenic acid (C) Pyridoxine (D) Niacin 491. Niacin or nicotinic acid is a monocarboxylic acid derivative of (A) Pyridine (B) Pyrimidine (C) Flavin (D) Adenine 492. Niacin is synthesized in the body from (A) Tryptophan  (B) Tyrosine (C) Glutamate (D) Aspartate 493. The proteins present in maize are deficient in (A) Lysine (B) Threonine (C) Tryptophan (D) Tyrosine 494. Niacin is present in maize in the form of (A) Niatin (B) Nicotin (C) Niacytin (D) Nicyn 495. In the body 1 mg of niacin can be produced from (A) 60 mg of pyridoxine (B) 60 mg of tryptophan (C) 30 mg of tryptophan (D) 30 mg of pantothenic acid 496. Pellagra occurs in population dependent on (A) Wheat (B) Rice (C) Maize (D) Milk 497. The enzymes with which nicotinamide act as coenzyme are (A) Dehydrogenases (B) Transaminases (C) Decarboxylases (D) Carboxylases 498. Dietary requirement of Vitamin D: (A) 400 I.U. (B) 1000 I.U. (C) 6000 I.U. (D) 700 I.U. 499. The Vitamin which does not contain a ring in the structure is (A) Pantothenic acid (B) Vitamin D (C) Riboflavin (D) Thiamin 500. Pantothenic acid is a constituent of the coenzyme involved in  (A) Decarboxylation (B) Dehydrogenation (C) Acetylation (D) Oxidation 501. The compound which has the lowest density is (A) Chylomicron (B) β-Lipoprotein (C) α-Lipoprotein (D) pre β-Lipoprotein 502 Non steroidal anti inflammatory drugs, such a s aspirin act by inhibiting activity of the enzyme: (A) Lipoxygenase (B) Cyclooxygenase (C) Phospholipase A2 (D) Lipoprotein lipase 503. From arachidonate, synthesis of prostaglandins is catalysed by (A) Cyclooxygenase (B) Lipoxygenase (C) Thromboxane synthase (D) Isomerase 504. A Holoenzyme is (A) Functional unit (B) Apo enzyme (C) Coenzyme (D) All of these 505. Gaucher’s disease is due to the deficiency of the enzyme: (A) α-Fucosidase (B) β-Galactosidase (C) β -Glucosidase (D) Sphingomyelinase 506. Neimann-Pick disease is due to the deficiency of the enzyme: (A) Hexosaminidase A and B (B) Ceramidase (C) Ceramide lactosidase (D) Sphingomyelinase 507. Krabbe’s disease is due to the deficiency of the enzyme: (A) Ceramide lactosidase (B) Ceramidase (C) β -Galactosidase  (D) GM1 β -Galactosidase 508. Fabry’s disease is due to the deficiency of the enzyme: (A) Ceramide trihexosidase (B) Galactocerebrosidase (C) Phytanic acid oxidase (D) Sphingomyelinase 509. Farber’s disease is due to the deficiency of the enzyme: (A) α-Galactosidase (B) Ceramidase (C) β -Glucocerebrosidase (D) Arylsulphatase A. 510. A synthetic nucleotide analogue, used in organ transplantation as a suppressor of immunologic rejection of grafts is (A) Theophylline (B) Cytarabine (C) 4-Hydroxypyrazolopyrimidine (D) 6-Mercaptopurine 511. Example of an extracellular enzyme is (A) Lactate dehydrogenase (B) Cytochrome oxidase (C) Pancreatic lipase (D) Hexokinase 512. Enzymes, which are produced in inactive form in the living cells, are called (A) Papain (B) Lysozymes (C) Apoenzymes (D) Proenzymes 513. An example of ligases is (A) Succinate thiokinase (B) Alanine racemase (C) Fumarase (D) Aldolase 514 An example of lyases is (A) Glutamine synthetase (B) Fumarase (C) Cholinesterase (D) Amylase  515. Activation or inactivation of certain key regulatory enzymes is accomplished by covalent modification of the amino acid: (A) Tyrosine (B) Phenylalanine (C) Lysine (D) Serine 516. The enzyme which can add water to a carbon-carbon double bond or remove water to create a double bond without breaking the bond is (A) Hydratase (B) Hydroxylase (C) Hydrolase (D) Esterase 517. Fischer’s ‘lock and key’ model of the enzyme action implies that (A) The active site is complementary in shape to that of substance only after interaction. (B) The active site is complementary in shape to that of substance (C) Substrates change conformation prior to active site interaction (D) The active site is flexible and adjusts to substrate 518. From the Lineweaver-Burk plot of Michaelis-Menten equation, Km and Vmax can be determined when V is the reaction velocity at substrate concentration S, the X- axis experimental data are expressed as (A) 1/V (B) V (C) 1/S (D) S 519. A sigmoidal plot of substrate concentration ([S]) verses reaction velocity (V) may indicate (A) Michaelis-Menten kinetics (B) Co-operative binding (C) Competitive inhibition (D) Non-competitive inhibition 520. The K m of the enzyme giving the kinetic data as below is (A) –0.50 (B) –0.25 (C) +0.25 (D) +0.33 521. The kinetic effect of purely competitive inhibitor of an enzyme (A) Increases Km without affecting Vmax (B) Decreases Km without affecting Vmax  (C) Increases Vmax without affecting Km (D) Decreases Vmax without affecting Km 522. If curve X in the graph (below) represents no inhibition for the reaction of the enzyme with its substrates, the curve representing the competitive inhibition, of the same reaction is (A) A (B) B (C) C (D) D 523. An inducer is absent in the type of enzyme: (A) Allosteric enzyme (B) Constitutive enzyme (C) Co-operative enzyme (D) Isoenzymic enzyme 524. A demonstrable inducer is absent in (A) Allosteric enzyme (B) Constitutive enzyme (C) Inhibited enzyme (D) Co-operative enzyme 525. In reversible non-competitive enzyme activity inhibition (A) Vmax is increased (B) Km is increased (C) Km is decreased (D) Concentration of active enzyme is reduced 526. In reversible non-competitive enzyme activity inhibition (A) Inhibitor bears structural resemblance to substrate (B) Inhibitor lowers the maximum velocity attainable with a given amount of enzyme (C) Km is increased (D) Km is decreased 527. In competitive enzyme activity inhibition (A) The structure of inhibitor generally resembles that of the substrate (B) Inhibitor decreases apparent Km (C) Km remains unaffective (E) Inhibitor decreases Vmax without affecting Km 528. In enzyme kinetics V max reflects (A) The amount of an active enzyme (B) Substrate concentration (C) Half the substrate concentration (D) Enzyme substrate complex  529. In enzyme kinetics Km implies (A) The substrate concentration that gives one half Vmax (B) The dissocation constant for the enzyme substrate comples (C) Concentration of enzyme (D) Half of the substrate concentration required to achieve Vmax 530. In competitive enzyme activity inhibition (A) Apparent Km is decreased (B) Apparent Km is increased (C) Vmax is increased (D) Vmax is decreased 531. In non competitive enzyme activity inhibition, inhibitor (A) Increases Km (B) Decreases Km (C) Does not effect Km (D) Increases Km 532. An enzyme catalyzing oxidoreduction, using oxygen as hydrogen acceptor is (A) Cytochrome oxidase (B) Lactate dehydrogenase (C) Malate dehydrogenase (D) Succinate dehydrogenase 533. The enzyme using some other substance, not oxygen as hydrogen acceptor is (A) Tyrosinase (B) Succinate dehydrogenase (C) Uricase (D) Cytochrome oxidase 534. An enzyme which uses hydrogen acceptor as substrate is (A) Xanthine oxidase (B) Aldehyde oxidase (C) Catalase (D) Tryptophan oxygenase 535. Enzyme involved in joining together two substrates is (A) Glutamine synthetase (B) Aldolase (C) Gunaine deaminase (D) Arginase 536. The pH optima of most of the enzymes is (A) Between 2 and 4 (B) Between 5 and 9 (C) Between 8 and 12 (D) Above 12 537. Coenzymes are (A) Heat stable, dialyzable, non protein organic molecules (B) Soluble, colloidal, protein molecules (C) Structural analogue of enzymes (D) Different forms of enzymes 538. An example of hydrogen transferring coenzyme is (A) CoA (B) NAD+ (C) Biotin (D) TPP 539. An example of group tra nsferri ng coenzyme is (A) NAD+ (B) NADP+ (C) FAD (D) CoA 540. Cocarboxylase is (A) Thiamine pyrophosphate (B) Pyridoxal phosphate (C) Biotin (D) CoA 541. A coenzyme containing non aromatic hetero ring is (A) ATP (B) NAD (C) FMN (D) Biotin 542. A coenzyme containing aromatic hetero ring is (A) TPP (B) Lipoic acid (C) Coenzyme Q (D) Biotin 543. Isoenzymes are (A) Chemically, immunologically and electrophoretically different forms of an enzyme (B) Different forms of an enzyme similar in all properties (C) Catalysing different reactions (D) Having the same quaternary structures like the enzymes 544. Isoenzymes can be characterized by (A) Proteins lacking enzymatic activity that are necessary for the activation of enzymes (B) Proteolytic enzymes activated by hydrolysis (C) Enzymes with identical primary structure  (D) Similar enzymes that catalyse different reaction 545. The isoenzymes of LDH (A) Differ only in a single amino acid (B) Differ in catalytic activity (C) Exist in 5 forms depending on M and H monomer contents (D) Occur as monomers 546. The normal value of CPK in serum varies between (A) 4–60 IU/L (B) 60–250 IU/L (C) 4–17 IU/L (D) > 350 IU/L 547. Factors affecting enzyme activity: (A) Concentration (B) pH (C) Temperature (D) All of these 548. The normal serum GOT activity ranges from (A) 3.0–15.0 IU/L (B) 4.0–17.0 IU/L (C) 4.0–60.0 IU/L (D) 0.9–4.0 IU/L 549. The normal GPT activity ranges from (A) 60.0–250.0 IU/L (B) 4.0–17.0 IU/L (C) 3.0–15.0 IU/L (D) 0.1–14.0 IU/L 550. The normal serum acid phosphatase activity ranges from (A) 5.0–13.0 KA units/100 ml (B) 1.0–5.0 KA units/100 ml (C) 13.0–18.0 KA units/100 ml (D) 0.2–0.8 KA units/100 ml 551. The normal serum alkaline phosphatase activity ranges from (A) 1.0–5.0 KA units/100 ml (B) 5.0–13.0 KA units/100 ml (C) 0.8–2.3 KA units/100 ml (D) 13.0–21.0 KA units/100 ml 552. In early stages of myocardial ischemia the most sensi tiv e indicator is the measurement of the activity of (A) CPK (B) SGPT  (C) SGOT (D) LDH 553. Serum acid phosphatase level increases in (A) Metastatic carcinoma of prostate (B) Myocardial infarction (C) Wilson’s disease (D) Liver diseases 554. Serum alkaline phosphatase level increases in (A) Hypothyroidism (B) Carcinoma of prostate (C) Hyperparathyroidism (D) Myocardial ischemia 555. Serum lipase level increases in (A) Paget’s disease (B) Gaucher’s disease (C) Acute pancreatitis (D) Diabetes mellitus 556. Serum ferroxidase level decreases in (A) Gaucher’s disease (B) Cirrhosis of liver (C) Acute pancreatitis (D) Wilson’s disease 557. The isoenzymes LDH5 is elevated in (A) Myocardial infarction (B) Peptic ulcer (C) Liver disease (D) Infectious diseases 558. On the third day of onset of acute myocardial infarction the enzyme elevated is (A) Serum AST (B) Serum CK (C) Serum LDH (D) Serum ALT 559. LDH1 and LDH2 are elevated in (A) Myocardial infarction (B) Liver disease (C) Kidney disease (D) Brain disease 560. The CK isoenzymes present in cardiac muscle is (A) BB and MB  (B) MM and MB (C) BB only (D) MB only 561. In acute pancreatitis, the enzyme raised in first five days is (A) Serum amylase (B) Serum lactic dehydrogenase (C) Urinary lipase (D) Urinary amylase 562. Acute pancreatitis is characterised by (A) Lack of synthesis of zymogen enzymes (B) Continuous release of zymogen enzymes into the gut (C) Premature activation of zymogen enzymes (D) Inactivation of zymogen enzymes 563. An example of functional plasma enzyme is (A) Lipoprotein lipase (B) Amylase (C) Aminotransferase (D) Lactate dehydrogenase 564. A non-functional plasma enzyme is (A) Psudocholinesterase (B) Lipoprotein lipase (C) Proenzyme of blood coagulation (D) Lipase 565. The pH optima for salivary analyse is (A) 6.6–6.8 (B) 2.0–7.5 (C) 7.9 (D) 8.6 566. The pH optima for pancreatic analyse is (A) 4.0 (B) 7.1 (C) 7.9 (D) 8.6 567. The pH optima for sucrase is (A) 5.0–7.0 (B) 5.8–6.2 (C) 5.4–6.0 (D) 8.6 568. The pH optima for maltase is (A) 1.0–2.0  (B) 5.2–6.0 (C) 5.8–6.2 (D) 5.4–6.0 569. The pH optima for lactase is (A) 1.0-2.0 (B) 5.4–6.0 (C) 5.0–7.0 (D) 5.8–6.2 570. The substrate for amylase is (A) Cane sugar (B) Starch (C) Lactose (D) Ribose 571. The ion which activates salivary amylaseactivity is (A) Chloride (B) Bicarbonate (C) Sodium (D) Potassium 572. The pancreatic amylase activity is increased in the presence of (A) Hydrochloric acid (B) Bile salts (C) Thiocyanate ions (D) Calcium ions 573. A carbohydrate which can not be digested in human gut is (A) Cellulose (B) Starch (C) Glycogen (D) Maltose 574. The s u g a r absorbed by facilitated diffusion and requiring Na independent transporter is (A) Glucose (B) Fructose (C) Galactose (D) Ribose 575. In the intestine the rate of absorption is highest for (A) Glucose and galactose (B) Fructose and mannose (C) Fructose and pentose (D) Mannose and pentose 576. Glucose absorption is promoted by (A) Vitamin A  (B) Thiamin (C) Vitamin C (D) Vitamin K 577. The harmone acting directly on intestinal mucosa and stimulating glucose absorption is (A) Insulin (B) Glucagon (C) Thyroxine (D) Vasopressin 578. Given that the standard free energy change (∆G°) for the hydrolysis of ATP is –7.3 K cal/mol and that for the hydrolysis of Glucose 6-phosphate is –3.3 Kcal/mol, the ∆G° for the phosphorylation of glucose is Glucose + ATP → Glucose 6– Phosphate + ADP. (A) –10.6 Kcal/mol (B) –7.3 Kcal/mol (C) –4.0 Kcal/mol (D) +4.0 Kcal/mol 579. At low blood glucose concentration, brain but not liver will take up glucose. It is due to the (A) Low Km of hexokinase (B) Low Km of glucokinase (C) Specificity of glucokinase (D) Blood brain barrier 580. In the reaction below, Nu TP stands for NuTP + glucose → Glucose 6–Phosphate + NuDP. (A) ATP (B) CTP (C) GTP (D) UTP 581. In the figures shown below, fructose 1,6-biphosphate is located at point: (A) A (B) B (C) C (D) D 582. The enzyme of the glycolic pathway, sensitive to inhibiton by fluoride ions is