MCQs in Biochemistry


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Copyright © 2008, New Age International (P) Ltd., Publishers
Published by New Age International (P) Ltd., Publishers
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FOREWORD
FOREWORD
FOREWORD
FOREWORD
WATER AND ELECTROLYTE BALANCE
PREFPREF
PREFPREF
AA
AA
CECE
CECE
I have brought out this book basically for students who plan to appear for Biochemistry in the entrance examinations like
JIPMER and other Medical, Pharmacy, Physiotherapy, Nursing and other Paramedical PG Entrance Examinations. There
is a dearth of good entrance manual of Biochemistry for the above said examinations. Hence, I have prepared an
AA
AA
SOME VSOME V
SOME VSOME V
ALUALU
ALUALU
This book is very useful for students appearing for GATE Exams. Recommended reading.
Prof. Dr. Subhas C. Marihal
Principal, Goa College of Pharmacy, Goa.
Biochemistry made simple in the form of multiple choice questions. Strongly recommended.
Prof. Dr. Vijaykumar Ishwar Hukkeri
Principal, KLE College of Pharmacy, Hubli
Dr. Vidya Sagar can be applauded for his untiring efforts in bringing out such a good book.
Recommended for students and Library
Dr. G. Devala Rao
Principal, Sidhartha College of Pharmaceutical Sciences
Vijaywada, A.P.
This book will be very useful companion for students appearing for PG Medical, Pharmacy, Nursing and
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I I
I I


TOTO
TOTO
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1.A drug which prevents uric acid synthesis
(A)Aspirin
(B)Allopurinol
(C)Colchicine(D)
2.Which of the following is required for
(A)Mn
(B)Mg
(C)Ca
(D)Zn
3.Oxidation of which substance in the body
(A)Glucose(B)Glycogen
(C)Protein
(D)Lipids
4.Milk is deficient in which vitamins?
(A)Vitamin C(B)Vitamin A
(C)Vitamin B
(D)Vitamin K
5.Milk is deficient of which mineral?
(A)Phosphorus
(B)Sodium
(C)Iron(D)Po
6.Synthesis of prostaglandinsis is inhibited
(A)Aspirin
(B)Arsenic
(C)Fluoride(D)Cyanide
MCQs IN BIOCHEMISTRY
(D)The hydrocarbon chain of cholesterol projects
12.Which one is the heaviest particulate
(A)Nucleus(B)
(C)Cytoplasm(D)
13.Which one is the largest particulate of the
(A)Lysosomes
(B)Mitochondria
(C)Golgi apparatus
INTRODUCTION TO BIOCHEMISTRY
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
(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
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1.The general formula of monosaccharides
(A)C
(B)C
(C)C
(D)C
2.The general formula of polysaccharides
(A)(C
(B)(C
(C)(C
(D)(C
3.The aldose sugar is
(A)Glycerose
(B)Ribulose
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MCQs IN BIOCHEMISTRY
15.In glucose the orientation of the —H and
34. The constituent unit of inulin is
(A)Glucose
(B)Fructose
(C)Mannose(D)Galactose
35.The polysaccharide found in the
(A)Glucose
(B)Fructose
(C)Lactose
(D)Maltose
50.Osazones are not formed with the
(A)Glucose
(B)Fructose
(C)Sucrose(D)
51.The most abundant carbohydrate found
(A)Starch
(B)Glycogen
(C)Cellulose (D)
52.Impaired renal function is indicated when
MCQs IN BIOCHEMISTRY
(A)Anomeric carbon atom
(B)Epimeric carbon atom
(C)Isomeric carbon atom
(D)None of these
73.The smallest monosaccharide having
(A)Erythrose(B)Ribose
(C)Glucose
(D)Fructose
74.Which of the following is an epimeric pair?
(A)Glucose and fructose
(B)Glucose and galactose
(C)Galactose and mannose
(D)Lactose and maltose
αα
αα
(A)Lactose
(B)Maltose
(C)Sucrose(D)
76.Branching occurs in glycogen approxi-
(A)Five glucose units
(B)Ten glucose units
(C)Fifteen glucose units
(D)Twenty glucose units
MCQs IN BIOCHEMISTRY
91.Debranching enzyme is absent in
(A)Cori’s disease
(B)Andersen’s disease
(C)Von Gierke’s disease
(D)Her’s disease
92.McArdle’s disease is due to the deficiency
(A)Glucose-6-phosphatase
(B)Phosphofructokinase
(C)Liver phosphorylase
(D)muscle phosphorylase
93.Tautomerisation is
(A)Shift of hydrogen(B)Shift of carbon
(C)Shift of both(D)None of these
94. In essential pentosuria, urine contains
(A)D-Ribose(B)D-Xylulose
(C)L-Xylulose
(D)D-Xylose
95.Action of salivary amylase on starch leads
(A)Maltose(B)
(C)Both of the above(D)Neither of these
96.Congenital galactosaemia can lead to
(A)Monosaccharides(B)Dissaccharides
(C)Polysaccharides(D)
(A)Hypertension
MCQs IN BIOCHEMISTRY
(A)Vitamins(B)
(C)Minerals(D)Nucleoproteins
(A)Gluconic acid(B)Saccharic acid
(C)Saccharo Lactone
(D)Mucic acid
(A)Triose isomerase
(B)Phosphotriose isomerase
(C)Diphosphotriose isomerase
MCQs IN BIOCHEMISTRY
(C)Pentose sugars and 4 membered sugars
(D)Pentose sugars and sedoheptulose
αα
αα
180 Dehydrogenase enzymes of the hexose
(A)NAD
specific(B)NADP
(C)FAD specific(D)FMN specific
of ATP.
(A)One
(B)Two
(C)Eight
(D)
(A)UDPG transferase
(B)Branching enzyme
(C)Phosphorylase
(D)Phosphatase
involved in glycolysis?
(A)Euolase
(B)Aldolose
(C)Hexokinase(D)
184.T
MCQs IN BIOCHEMISTRY
(A)Aerobic glycolysis
(B)Oxidation
(C)Oxidative phosphorylation
(D)Anaerobic glycolysis
(A)6(B)3
(C)1(D)2
(A)6
(B)1
(C)2
(D)3
(A)Glucokinase, Pyruvate carboxylae
(B)Pyruvate carboxylase, phosphoenol pyruvate
(C)Pyruvate kinase, pyruvate carboxylase,
(D)Phospho fructokinase, pyruvate carboxylase,
199.For glycogen
(A)Glucuronic acid(B)Pyruvic acid
(C)UDP glucose(D)
(A)Glyceraldehyde-3-phosphate dehydrogenase
(B)Aconitase
(C)Enolose
(D)Succinate dehydrogenase
One of the following statement is correct:
(A)Glycogen synthase ‘a’ is the phosphorylated
(B)cAMP converts glycogen synthase b to ‘a’
(C)Insulin converts glycogen synthase b to a
(D)UDP glucose molecules interact and grow into
(A)Branching enzyme
(B)debranching enzyme
(C)Glucantransferase
(D)Phosphorylase
(A)insulin independent transport
(B)insulin dependent transport
(C)enzyme mediated transport
(D)Both (A) and (B)
204.
(A)Glucose
(B)Glucose 1-phosphate and Glycogen with 1
(C)Glucose-6-phosphate and Glycogen with 1
(D)6-Phosphogluconic acid
(A)Phosphopyruvate(B)
(A)Hexokinase
(B)Phsophofructokinase
(C)Pyruvate carboxylase
(D)Pyruvate kinase
The number of ATP produced in the
(A)1
(B)2
(C)3
(D)4
lactose?
(A)UDP galactose and glucose
(B)UDP glucose and galactose
(C)Glucose and Galactose
(D)Glucose, Galactose and UTP
(A)Chondroitin sulphates
(B)Glycogen
(C)Lactose
(D)Starch
(A)Albino rats(B)Humans
(C)Monkeys(D)
215.Which one of
(A)Albino rats(B)Dogs
(C)Monkeys(D)
216.T
MCQs IN BIOCHEMISTRY
(A)Contain many monosaccharide units which
(B)Function mainly a storage or structural
(C)Are present in large amounts in connective
(D)All of these
(A)Occurs in the small intestine
(B)Is stimulated by the hormone Glucagon
(C)Occurs more rapidly than the absorption of
242.Which of the following is a
(A)Glyceraldehyde-3-p
(B)Glucose-6-p
(C)Fructose-6-p
(D)Fructose1,6-bisphosphate
243.The ratio that approximates the number
MCQs IN BIOCHEMISTRY
(A)To lose electrons
(B)To gain electrons
(C)To lose/gain electrons
(D)To lose and gain electrons
257.E
(A)Electrons(B)Protons
(C)Uncouplers(D)
(A)Lose electrons
(B)Gain electrons
(C)Lose (or) gain electrons
(D)Lose and gain electrons
of terminal phosphate group of ATP is
(A)–7,300 cal/mol(B)–8,300 cal/mol
(C)10,000 cal/mol(D)+7,300 cal/mol
(A)–52,580 cal(B)–50,580 cal
(C)21,900 cal(D)+52,580 cal
ATP from 3 ADP and 3 pi is
(A)–21,900 cal(B)29,900 cal
(C)31,900 cal(D)39,900 cal
(A)Is directly proportional to the standard free
(B)Is equal to zero at equilibrium
(C)Can only be calculated when the reactants
(D)Is equal to –RT in keq
(A)The free energy change
(B)The standard free energy change
(C)The free energy change,
(D)Keq is equal to 1
264.An
(A)Inhibits electron transport and ATP synthesis
(B)Allow electron transport to proceed without
ATP synthesis
(C)Inhibits electron transport without impairment
of ATP synthesis
(D)Specially inhibits cytochrome b
synthesis of ATP during oxidative
(A)It is located on the matrix side of the inner
(B)It is inhibited by oligomycin
(C)It can exhibit ATPase activity
(D)It can bind molecular O
(A)Is widely distributed and occurs in most
(B)Has a high k
important in the phosphorylation of glucose
(C)Is widely distributed in Prokaryotes
(D)None of these
(A)Is activated by high concentrations of ATP and
(B)Uses fruitose-1-phosphate as substrate
(C)Is the rate-limiting reaction of the glycolytic
(D)Is inhibited by fructose 2, 6-bisphosphate
(A)An increased conversion of pyruvate to lactate
(B)Decreased oxidation of pyruvate of CO
(C)A decreased NADH/NAD
(D)Decreased concentration of AMP
expected in pyruvate kinase deficiency?
(A)Increased levels of lactate in the R.B.C
(B)Hemolytic anemia
(C)Decreased ratio of ADP to ATP in R.B.C
(D)Increased phosphorylation of Glucose to
MCQs IN BIOCHEMISTRY
284.The general formula for polysaccharide is
(A)(C
(B)(C
(C)(C
(D)(C
285.Epimers of gluc
(A)Fructose(B)
(C)Ribose
(D)Deoxyribose
(A)D-Arabinose(B)D-Ribose
(C)D-Xylose(D)L-Xylose
(A)D-Ribulose(B)D-Arabinose
(C)D-xylose(D)
D-Lyxose
288.On
boiling Benedict’s solution is not
(A)Sucrose(B)
(C)Maltose(D)
289.The
5. B
8. D
10. A
11. A
12. C
22. D
26. D
31. D
37. C
38. B
40. A
41. D
42. B
44. B
57. D
60. D
63. B
67. B
68. C
70. D
71. A
72. A
79. A
80. B
82. C
83. D
84. D
85. B
88. C
89. B
90. A
92. D
96. D
98. A
99. C100. C
101. B102. A
103. C104. C
C108. D
109. B110. C
113. B114. D
115. B116. B
117. A118. B
119. B120. A
121. B122. D
125. C126. A
127. B128. D
129. C130. A
131. A132. D
133. C134. B
135. C136. C
137. C138. A
139. B140. C
143. C144. D
145. B146. C
149. B150. D
151. B152. C
153. D154. A
155. B156. A
157. C158. A
161. A162. B
163. A164. B
165. D
167. C168. A
169. B170. A
171. D
173. A174. B
175. D176. B
177. A178. C
179. D180. B
181. B182. C
183. D184. B
185. C186. C
187. A188. B
191. A192. D
193. D194. C
195. D196. A
197. B198. B
199. C200. C
D204. C
205. C206. D
209. C210. C
211. B212. A
213. A214. A
215. C216. C
217. C218. C
219. C220. B
222.C
223. B224. B
227. D228. A
229. B230. D
231. C232. B
233. C234. A
235. B236. D
239. B240. C
241. D242. D
243. B
245. D246. A
247. D248. D
250. B
251. D252. D
MCQs IN BIOCHEMISTRY
253. A254. A
255. C256. A
257. B258. B
259. A260. D
263. C264. B
265. D266. B
267. C268. A
269. B270. C
271. B272. C
D276. C
277. D278. C
279. D280. A
281. C282. B
283. C284. A
285. B286. C
287. A288. A
289. C290. C
291. D292. B
293. C294. B
295. C296. A
299. B300. D
301. C302. D
7. APolysaccharides are polymers of monosac-
charides. They are of two types– hompolysac-
251. DThe three enzymes namely hexokinase (or
phosphofructokinase is the most regulatory. It
is an allosteric enzyme inhibited by ATP, citrate
by ATP and citrate (formed in the presence of
291. DThe cycle involving the synthesis of glucose in
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1.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
2.Proteins contain
(A)Only L-
(B)Only D-amino acids
(C)DL-Amino acids
(D)Both (A)
3.The optically inactive amino acid is
(A)Glycine(B)Serine
(C)Threonine(D)
Valine
4.At neutral pH, a mixture of amino acids
(A)Dipolar ions
(B)Nonpolar molecules
(C)Positive and monovalent
(D)Hydrophobic
5.The true statement about solutions of
(A)All amino acids contain both positive and
(B)All amino acids contain positively charged
(C)Some amino acids contain only positive
CHAPTER 3
CHAPTER 3
CHAPTER 3
CHAPTER 3
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MCQs IN BIOCHEMISTRY
12.The functions of plasma albumin are
(A)Osmosis(B)
Transport
(C)Immunity(D)
13.Amino acid with side chain containing
(A)2-Amino 5-guanidovaleric acid
(B)2-Pyrrolidine carboxylic acid
(C)2-Amino 3-mercaptopropanoic acid
(D)2-Amino propanoic acid
14.An example of
αα
αα
32.A peptide which acts as potent smooth
(A)Glutathione(B)
(C)Tryocidine(D)
33.A tripeptide functioning as an important
(A)Bradykinin(B)
(C)Tyrocidin(D)
MCQs IN BIOCHEMISTRY
67.Ceruloplasmin is
-globulin(B)
-globulin(D)None
68.The lipoprotein with the fastest electro-
MCQs IN BIOCHEMISTRY
ββ
ββ
(A)0.95–1.006(B)1.006–1.019
(C)1.019–1.063(D)1.063–1.125
86.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
87.Aspirin inhibits the activity of the enzyme:
(A)Lipoxygenase(B)
(C)Phospholipae A
(D)Phospholipase A
88.A ’suicide enzyme’ is
(A)Cycloxygenase
(B)Lipooxygenase
(C)Phospholipase A
(D)Phospholipase A
89.In adipose tissue prostaglandins
(A)Lipogenesis(B)
(C)Gluconeogenesis(D)
90The 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
91.Pepsinogen is converted to active pepsin
(A)HCl
(B)Bile salts
(C)Ca
(D)Enterokinase
92.The optimal pH for the enzyme rennin is
(A)2.0
(B)4.0
(C)8.0
(D)6.0
93.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
94.The optimal pH for the enzyme chymo-
(A)2.0
(B)4.0
(C)6.0
(D)8.0
95Trypsinogen is converted to active trypsin
(A)Enterokinase(B)
(C)HCl
(D)Mg
96Pepsin acts on denatured proteins to
(A)Proteoses and peptones
(B)Polypeptides
(C)Peptides
(D)Dipeptides
97.Renin converts casein to paracasein in
(A)Ca
(B)Mg
(C)Na
(D)K
98.An expopeptidase is
(A)Trypsin
(B)Chymotrypsin
(C)Elastase(D)Elastase
99.The enzyme trypsin is specific for peptide
(A)Basic amino acids
(B)Acidic amino acids
(C)Aromatic amino acids
(D)Next to small amino acid residues
100.Chymotrypsin is specific for peptide bonds
(A)Uncharged amino acid residues
(B)Acidic amino acids
(C)Basic amino acid
(D)Small amino acid residues
G.I.T. is
(A)Dipeptide(B)T
(C)Polypeptide(D)
(A)Passive diffusion(B)Simple diffusion
(C)Faciliated diffusion(D)Active process
(A)Haemophilia(B)Christmas disease
(C)Gout
(D)
104.An
(A)Thiamin
(B)Riboflavin
(C)Niacin
(D)
(A)Liver and kidney
(B)Skin and pancreas
(C)Intestine and mammary gland
(D)Lung and spleen
106.A
(A)In growing infant
(B)Following surgery
(C)In advanced cancer
(D)In kwashiorkar
(A)Liver
(B)Skin
(C)Intestine(D)Kidney
(A)Mitochondria only
(B)Cytosol only
(C)Both mitochondria and cytosol
(D)Nucleus
The number of ATP required for urea
(A)0
(B)1
(C)2
(D)3
αα
αα
(A)L-glutamate dehydrogenase
(B)L-amino acid oxidase
(C)Histidase
(D)Serine dehydratase
111.In urea
MCQs IN BIOCHEMISTRY
ββ
ββ
(A)Vitamin A(B)Vitamin C
(C)Vitamin E
(D)Vitamin B
122.In
141.A
(A)Thiamin
(B)Ribofalvin
(C)Ascrobic acid(D)Cobalamin
(A)Lysine
(B)
MCQs IN BIOCHEMISTRY
163.At a pH
(A)Cation
(B)Anion
(C)Zwitterion
(D)Undissociated molecule
164.An am
(A)Alanine
(B)Proline
Edman’s reaction can be used to
MCQs IN BIOCHEMISTRY
(A)Glutamate and
215.A
(A)ATP(B)GTP
(C)ADP and GDP(D)AMP and GMP
(A)Oxidative deamination of glutamate
(B)Catabolism of purines
(C)Catabolism of pyrimidines
(D)All of these
217.An
(A)Liver(B)Brain
(C)Kidney(D)Heart
(A)Free ammonia(B)Glutamine
(C)Asparagine
(C)Alanine
(A)Brain
(B)Kidneys
(C)Liver
(D)
(A)Cytosol
(B)
(C)Both (A) and (B)(D)None of these
MCQs IN BIOCHEMISTRY
(A)Taurocholic
acid(B)
(C)Purines
(D)Pyrimidines
231.Histamine is for
(A)Deamination(B)Dehydrogenation
(C)Decarboxylation
(D)Carboxylation
232.DOPA is an inter
(A)Thyroid hormones
(B)Catecholamines
(C)Melanin
(D)Catecholamines and melanin
233.All the following stat
(A)It is smaller than pepsinogen
(B)It is formed by the action of HCl on its precursor
(C)Its optimum pH is 1.0–2.0
(D)It hydrolyses the C-terminal and N-terminal
(A)Trypsin
(B)Chymotrypsin
(C)Carboxypeptidase(D)
(A)It is formed from trypsin
(B)Carboxypeptidase converts trypsin into
chymotrypsin
(C)Its optimum pH is around 7
(D)It hydrolyses peptide bonds involving basic
(A)Hapten
(B)Epitope
(C)Complement(D)V
(A)They have high molecular weights
(B)They cannot elicit an immune response by
(C)When combined with some other large
(D)Once an immune response develops, the free
(A)They have high molecular weights
(B)They can elicit immune response by themselves
(C)They can elicit an immune response only in
(D)Once an immune response develops, free
(A)Two
(B)Four
(C)Five
(D)Six
(A)Alpha and kappa(B)Alpha and gamma
(C)Lambda and delta(D)Kappa and lambda
241Immunoglobulins are classified on the
(A)Type of light chains
(B)Type of heavy chains
(C)Types of light and heavy chains
(D)Molecular weight
(A)10,000–15,000(B)20,000–25,000
(C)25,000–50,000(D)50,000–75,000
(A)20,000–25,000(B)25,000–50,000
(C)50,000–70,000(D)70,000–1,00,000
(A)N-terminal quarter
(B)N-terminal half
(C)C-terminal quarter
(D)C-terminal half
(A)One hypervariable region
(B)Two hypervariable regions
(C)Three hypervariable regions
(D)Four hypervariable regions
(A)One hypervariable region
(B)Two hypervariable regions
(C)Three hypervariable regions
(D)Four hypervariable regions
(A)IgA
(B)IgG
(C)IgM
(D)IgD
(A)IgA
(B)IgG
(C)IgM
(D)IgD
(A)1–5 mg/dl(B)40–200 mg/dl
(C)60–500 mg/dl(D)700–1,500 mg/dl
252.An
MCQs IN BIOCHEMISTRY
(A)The classical pathway of complement fixation
(B)The alternate complement pathway
(C)Both (A) and (B)
(D)None of these
doesn’t involve
(A)Antigen-antibody complex
(B)Complement 3
(C)Factors B and D
(D)Membrane attack unit
(A)Gene amplification
(B)Gene re-arrangement
(C)Alternative splicing
(D)All of these
267.A
(A)Variable and constant segments
(B)Variable, joining and constant segments
(C)Variable, diversity and constant segments
(D)Variable, joining, diversity and constant
268.In
(A)All cells
(B)B lymphocytes only
(C)Macrophages only
(D)Macrophages and B lymphocytes
(A)Cytotoxic T cells
(B)Helper T cells
(C)Suppressor T cells
(D)Memory T cells
284.CD 8 is a
(A)Cytotoxic T cells
(B)Helper T cells
(C)Suppressor T cells
(D)Memory T cells
285.CD 4 is a
(A)Cytotoxic T cells(B)
(C)Suppressor T cells(D)Memory T cells
286.CD 3
(A)Cytotoxic T cells(B)
(C)Both (A) and (B)(D)None of these
287.Cytotoxic T ce
(A)Perforins
(B)Interleukins
(C)Colony stimulating factors
(D)Tumour necrosis factor
(A)Interleukins
(B)Colony stimulating factors
(C)Tumour necrosis factor
(D)All of these
(A)Immunoglobulins
(B)Components of complement system
(C)T cells receptors
(D)CD4 and CD8 proteins
(A)Cytotoxic T cells(B)
(C)B cells
(D)Plasma cells
291.In all
(A)IgA
(B)IgG
(C)IgD
(D)IgE
(A)Basophils(B)
(C)Both (A) and (B)(D)None of these
(A)IgA
(B)IgG
(C)IgD
(D)IgE
(A)Killed bacteria or viruses
(B)Live attenuated bacteria or viruses
(C)Toxoids
(D)All of these
(A)Pure antigens
(B)Immunoglobulins
(C)Toxoids
(D)Killed bacteria or viruses
(A)Interleukins
(B)Colony stimulating factors
(C)Perforins
(D)Tumour necrosis factor
(A)Two light and two heavy chains
(B)Two F
(C)Two pairs of one light and one heavy chain
(D)One F
(A)An immunoglobulin
(B)A dimer of heavy chains
(C)A dimer of light chains
(D)A dimer of one heavy and one light chains
MCQs IN BIOCHEMISTRY
(A)They are dimers of light chains
(B)Their amino acids sequences are identical
(C)Their N-terminal halves have variable amino
(D)Their C-terminal halves have constant amino
300.A
(A)Positive ion
(B)Negative ion
(C)Both (A) and (C)(D)None of these
(B)10% kcal are added on account of SDA
(C)20% kcal are subtracted on account of SDA
(D)20% kcal are subtracted on account of SDA
(A)1,900 kcal/day(B)2,400 kcal/day
(C)2,700 kcal/day(D)3,000 kcal/day
(A)1,900 kcal/day(B)2,200 kcal/day
(C)2,400 kcal/day(D)2,700 kcal/day
308.During pr
egnancy, the following should
(A)300 kcal/day(B)500 kcal/day
(C)700 kcal/day(D)900 kcal/day
(A)200 kcal/day(B)300 kcal/day
(C)550 kcal/day(D)1,000 kcal/day
315.B
(A)The percentage of ingested protein/nitrogen
(B)The percentage of ingested protein/nitrogen
(C)The percentage of ingested protein utilised
(D)The gain in body weight (gm) per gm of
MCQs IN BIOCHEMISTRY
(A)Calcium(B)
(C)Biotin(D)
(A)Essential amino acids
(B)Carbohydrates
(C)Avidin
(D)Biotin
(A)Milk
(B)Fish
(C)Egg white(D)Egg yolk
(A)Iron
(B)Fluorine
(C)Copper(D)Zinc
αα
αα
MCQs IN BIOCHEMISTRY
(A)Serine
(B)Pheny
(C)Tyrosine(D)Tr
(A)It causes vasolidatation
(B)It causes bronchoconstriction
(B)Mismatched blood transfusion
(C)Yellow fever
(D)Stone in urinary tract
383.Haematuria can occur in all of the following
(A)Acute glomerulonephritis
(B)Cancer of urinary tract
(C)Stone in urinary tract
(D)Mismatched blood transfusion
MCQs IN BIOCHEMISTRY
(A)Acute parotitis
(B)Acute pancreatitis
(C)Infective hepatitis(D)
Biliary obstr
(A)Lysine
(B)Ornithine
(C)Arginine
(D)Arginino succinic acid
(A)Optical rotation
(B)Dissociation constant
(C)Diffusion coefficient
(D)Chain length
418.When amino acids are treated with neutral
formaldehyde, the pH of the mixture
(A)Is not altered
(B)Increases
(C)Decreases
(D)First increases then decreases
(A)Histidine(B)
Tryptophan
(C)Proline
(D)
420.The
(A)solid state
(B)acidic solution
(C)alkaline solution(D)neutral solution
(A)Salting out(B)
MCQs IN BIOCHEMISTRY
(A)Glycine(B)Serine
(C)Aspartic acid
(D)Glutamic acid
(A)Glycine(B)Serine
(C)Threonine(D)
Tryptophan
(A)20
(B)25
(C)40
(D)35
(A)D
(B)L
(C)DL
(D)All of these
(A)1
(B)2
(C)3
(D)4
(A)Lysine
(B)
(C)Leucine(D)
(A)Alanine
(B)Isoleucine
(C)Arginine(D)Threonine
(A)Homoserine(B)Serine
453.T
nation of alanine with
(A)
MCQs IN BIOCHEMISTRY
(A)Dopa decarboxylation
(B)Diamine oxidase
(C)Peroxidase
(D)Tyrosinase
471.In one of
485.Optically active compounds are capable of
(A)Different reactions
(B)Rotating plane of polarized light
(C)Showing same chemical properties
(D)None of these
486.The reference compound for absolute confi-
(A)Alanine(B)Lactic acid
(C)Glyceraldehyde(D)
MCQs IN BIOCHEMISTRY
(A)NaHCO
(B)NaHCO
(C)NaHCO
(D)None of these
503.In
HN––COO——HN––COOH
(A)Acid
(B)Base
(C)Zwitter ion(D)
(A)They exist as zwitter ions
(B)Their pk and not in the physiological pH of a
(C)Only Histidine has pk of its R group at 6.0
(D)None of these
505.At
HNCCOOH
HNCCOO
HNCCOO
HNCCOO
(A)An intracellular enzyme
(B)Serum enzyme
MCQs IN BIOCHEMISTRY
538.A
(A)Filtration(B)
(C)Oxidation(D)
(A)Performic acid(B)Oxalic acid
(C)Citric acid(D)M
(A)Weak
(B)Strong
(C)Both (A) and (B)(D)None of these
561.A
(A)Globular pr
(B)Fibrous proteins
(C)Both (A) and (B)(D)None of these
562.In
(B)
(C)Both (A) and (B)(D)None of these
(A)Hydrogen bonds(B)Salt bonds
(C)Non-polar bonds(D)Disulphide bonds
αα
αα
(A)2.8
(B)3.2
(C)3.4
(D)3.6
αα
αα
(A)0.34
(B)0.44
(C)0.54
(D)0.64
αα
αα
(A)Proline
(B)Arginine
(C)Histidine(D)
Lysine
αα
αα
(A)Hydrogen bonds(B)Disulphide bonds
(C)Salt bonds(D)Non-polar bonds
MCQs IN BIOCHEMISTRY
576.In glycoproteins the carbohydrate is in the
(A)50–100(B)200–300
(C)400–500(D)600–700
(A)Pepsin
(B)Tr
(C)Chymotrypsin(D)
578.
(A)Pepsin only(B)Both pepsin and HCl
(C)HCl only(D)
(A)Hemolytic anemia(B)Pernicious anemia
(C)Both (A) and (B)(D)None of these
580.In
(A)Arginine(B)Histidine
(C)Serine(D)
(A)Alanine(B)
(C)Valine
(A)Ammonia
(B)Urea
(C)Ammonium salts(D)Uric acid
(A)The bases of the phospholipids
(B)Uric acid
(C)Glycolipids
(D)Chondroitin sulphates
MCQs IN BIOCHEMISTRY
(A)Acidosis(B)Alkalosis
(C)Both (A) and (B)(D)None of these
613.Amm
(A)Buffers
(B)Immunoglobulins
(C)Reserve proteins
(D)All of these
MCQs IN BIOCHEMISTRY
this technique:
(A)Solubility curve
(B)Solvent precipitation
667.Proteins which are responsible for defence
MCQs IN BIOCHEMISTRY
transfer of phosphate from ATP to pyruvic
(A)Sodium(B)Calcium
(C)Magnesium(D)
(A)Three classes
(B)Six classes
(C)Four classess(D)
Ten classes
688.Michaelis – Menten equation is used to
(A)Carbohydrate
(B)Enzyme
(C)Lipid
(D)Protein
689.The pH at which an enzyme has maximum
(A)Isoelectric pH(B)
(C)Low pH(D)High pH
(A)Anabolism
(A)Mg
(B)Zn
(C)Co
(D)Ca
MCQs IN BIOCHEMISTRY
(A)Salting out with (NH
(B)Ultracentrifugation
(C)Immuno electrophoresis
(D)All of these
(A)Uracil
(B)Adenine
11. B
12. A
24. D
33. D
48. B
49. D
53. D
61. B
62. A
63. D
64. C
66. C
68. D
72. B
77. D
78. D
84. D
94. D
98. D
99. A100. A
101. D102. D
103. D104. D
105. A
107. A108. C
109. D110. A
111. A112. A
113. A114. B
115. D116. C
117. A118. A
119. D120. C
121. B122. B
123. A124. A
125. A126. A
127. B128. C
129. A130. A
131. B132. C
133. A134. A
135. A136. A
137. C138. A
139. A140. D
143. C144. B
145. A146. B
147. B148. B
149. D150. A
151. A152. B
153. C154. C
155. B156. C
157. D158. D
159. C160. C
161. B162. D
163. A164. D
166. B
167. D168. D
169. C170. C
171. D172. B
173. A174. D
175. D176. C
177. B178. B
179. A180. A
181. C182. C
183. B184. C
185. B186. C
187. D188. A
189. B190. D
191. C192. C
193. B194. C
195. D196. B
197. D198. C
199. B200. B
C204. C
205. D206. C
207. D208. B
209. A210. D
211. C212. A
215. C216. D
217. B218. D
219. B220. B
221. C222. D
223. C224. C
C228. D
229. C230. A
231. C232. D
233. D234. D
235. C236. B
237. A238. D
239. B240. D
241. B242. B
243. C244. A
245. B246. A
247. C248. D
249. B250. C
251. C252. A
MCQs IN BIOCHEMISTRY
253. D254. D
255. D256. B
257. D258. B
259. D260. D
263. D264. B
265. A266. B
267. B268. D
269. B270. D
271. C272. B
D276. B
277. B278. D
279. C280. D
281. A282. D
283. B284. C
286. D
287. B288. B
289. D290. B
D294. D
295. B296. C
297. B298. C
299. B300. C
301. A302. B
303. B304. C
305. B306. B
307. A308. A
309. C310. D
311. B312. D
313. D314. C
315. B316. D
317. B318. B
319. D320. B
321. A322. B
323. D324. A
325. B326. B
B330. D
331. C332. D
333. C334. B
335. C336. B
337. C338. A
D342. B
343. A344. B
345. C346. B
349. B350. B
351. C352. C
353. B354. C
355. D356. D
357. C358. B
359. D360. D
361. B362. B
363. D364. B
365. D366. D
367. A368. C
369. A370. A
371. D372. B
373. B374. D
375. A376. B
377. A378. B
379. D380. B
383. D384. D
385. C386. A
C390. D
391. D392. D
C396. B
397. D398. B
399. B400. A
401. B402. A
403. B404. C
405. D406. D
407. B408. B
409. B410. D
413. C414. C
415. D416. C
417. B418. C
419. A420. D
421. D422. A
423. C424. D
425. D426. C
427. D428. D
429. A430. B
431. D432. A
433. B434. A
435. A436. A
437. B438. B
439. C440. D
441. C442. C
443. B444. D
445. C446. B
447. D448. C
449. C450. C
451. C452. D
455. B456. C
457. D458. C
459. A
461. B462. A
463. A464. C
467. B468. A
469. A470. D
473. A474. B
475. B476. D
477. C478. C
479. B480. D
481. C482. B
483. C484. B
485. B486. C
487. C488. D
489. B490. B
491. C492. C
493. B494. A
495. B496. B
497. A498. C
499. D500. D
501. C502. C
503. C504. C
505. B506. A
507. D
509. A510. C
511. B512. D
513. D514. A
515. A516. C
517. A518. D
519. A520. D
521. A522. D
523. C524. B
525. D526. A
527. B528. A
529. A530. B
531. D532. D
533. B534. A
535. B536. A
539. C540. A
541. C542. C
543. A544. D
545. D546. B
547. D548. A
549. A550. B
551. D552. B
553. A554. B
B558. D
559. A560. A
561. A562. A
563. D564. D
565. C566. A
567. A568. A
569. A570. B
571. A572. A
C576. D
577. D578. B
581. B582. C
583. C584. C
587. D588. B
589. A590. C
593. C594. D
595. B596. A
597. A598. C
599. D600. D
601. C602. C
603. B604. B
605. B606. A
607. A608. A
609. B610. A
611. C612. B
613. D614. A
615. D616. A
617. D618. B
619. D620. C
621. A
623. A624. B
625. D626. B
627. B628. B
629. D630. B
631. D632. D
633. A
635. D636. C
637. A638. A
639. C640. B
641. B642. B
643. D644. B
645. D646. D
647. B648. C
651. D652. A
653. B654. C
655. D656. A
659. C660. B
661. A662. D
663. C664. D
665. C666. B
667. B668. C
671. D672. A
673. C674. A
D678. B
679. C680. D
681. B682. B
683. A684. C
685. A686. D
689. B690. C
691. D692. C
693. D694. C
695. D696. D
697. A698. D
701. B702. C
703. C704. D
705. C706. B
707. A708. D
709. B710. C
713. D714. B
715. C716. D
719. B720. B
721. D722. C
723. D724. C
725. B726. C
727. B728.
MCQs IN BIOCHEMISTRY
synthesized by the liver. Plasma albumin
decreased in Wilson’s disease.
Christmas disease (defect-Christmas factor,
151. ALysine,
non-protein amino acids. However, the non-
268. DAmino acids are divided into 3 groups based
1.An example of a hydroxy fatty acid is
(A)Ricinoleic acid(B)Crotonic acid
(C)Butyric acid
(D)Oleic acid
2.An example of a saturated fatty acid is
(A)Palmitic acid(B)Oleic acid
(C)Linoleic acid(D)Erucic acid
3.If the fatty acid is esterified with an
(A)Lipositol(B)
(C)Wax
(D)Cephalin
4.A fatty acid which is not synthesized in
CHAPTER 4
CHAPTER 4
CHAPTER 4
CHAPTER 4
FF
FF
AA
AA
TSTS
TSTS


ANDAND
ANDAND


FF
FF
AA
AA
TTYTTY
TTYTTY


AA
AA
CIDCID
CIDCID


MM
MM
MCQs IN BIOCHEMISTRY
13.The importance of phospholipids as
(A)Fatty acids
(B)Both polar and nonpolar groups
(C)Glycerol
(D)Phosphoric acid
14.In neutral fats, the unsaponificable matter
(A)Hydrocarbons(B)Triacylglycerol
(C)Phospholipids(D)
15.Higher alcohol present in waxes is
(A)Benzyl
MCQs IN BIOCHEMISTRY
46.Neonatal tyrosinemia improves on admi-
(A)Thiamin
(B)Riboflavin
(C)Pyridoxine(D)
47.Absence of phenylalanine hydroxylase
(A)Neonatal tyrosinemia
61.Phrynoderma is a deficiency of
(A)Essential fatty
acids(B)Proteins
(C)Amino acids(D)
62.The percentage of linoleic acid in safflow-
(A)73
(B)57
(C)40
(D)15
63.The percentage of polyunsaturated fatty
(A)62
(B)10
(C)3
(D)2
64.The percentage of polyunsaturated fatty
(A)60
(B)37
(C)25
(D)3
MCQs IN BIOCHEMISTRY
79.The normal range of direct reacting
(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
80.The normal range of indirect (unconjugat-
(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
81.Jaundice is visible when serum bilirubin
(A)0.5 mg/100 ml(B)0.8 mg/100 ml
(C)1 mg/100 ml(D)2.4 mg/100 ml
82.An increase in serum unconjugated
(A)Hemolytic jaundice
(B)Obstructive jaundice
(C)Nephritis
(D)Glomerulonephritis
83.One of the causes of hemolytic jaundice is
(A)G-6 phosphatase deficiency
(B)Increased conjugated bilirubin
(C)Glucokinase deficiency
(D)Phosphoglucomutase deficiency
84.Increased urobilinogen in urine and
(A)Obstructive jaundice
(B)Hemolytic jaundice
(C)Viral hepatitis
(D)Toxic jaundice
85.A jaundice in which serum alanine
(A)Hepatic jaundice
(B)Hemolytic jaundice
(C)Parenchymatous jaundice
(D)Obstructive Jaundice
86.Fecal stercobilinogen is increased in
(A)Hemolytic jaundice
(B)Hepatic jaundice
(C)Viral hepatitis
(D)Obstructive jaundice
87.Fecal urobilinogen is increased in
(A)Hemolytic jaundice
(B)Obstruction of biliary duct
(C)Extrahepatic gall stones
(D)Enlarged lymphnodes
88.A mixture of conjugated and unconjugat-
(A)Hemolytic jaundice
(B)Hepatic jaundice
(C)Obstructive jaundice
(D)Post hepatic jaundice
89.Hepatocellular jaundice as compared to
(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
90.Icteric index of an normal adult varies
93.Fecal urobilinogen is decreased in
(A)Obstruction of biliary duct
(B)Hemolytic jaundice
(C)Excess fat intake
(D)Low fat intake
MCQs IN BIOCHEMISTRY
(A)Concentration of urea in urine in gm/24hr
(B)Concentration of urea in urine in mg/100 ml
(C)Concentration of urea in blood in mg/100 ml
(D)Volume of urine in ml/mt
110.A
(A)30 ml(B)50 ml
(C)75 ml(D)90 ml
(A)20 ml(B)30 ml
(C)40 ml(D)54 ml
(A)Acute nephritis
(B)Pneumonia
(C)Early stage of nephritic syndrome
(D)Benign hypertension
(A)Endogenous creatinine clearance
(B)Para-aminohippurate test
(C)Addis test
(D)Mosenthal test
114.At normal levels of
(B)Impairment of the capacity of the tubule to
(C)Impairment of renal plasma flow
(D)Glomerular filtration rate
PAH is
(A)20
(B)40
(C)60
(D)80
(A)0.10–0.15(B)0.16–0.21
(C)0.25–0.30(D)0.35–0.40
(A)Early essential hypertension
(B)Malignant phase of hypertension
(C)Glomerulonephritis
(D)Acute nephritis
(A)Glomerulonephritis
(B)Malignant phase of hypertension
(C)Early essential hypertension
(D)Acute nephritis
(A)Glomerulonephritis
(B)Early essential hypertension
(C)Malignant phase of hypertension
(D)Starvation
MCQs IN BIOCHEMISTRY
All the following are omega-6-fatty acids
(A)Linoleic acid(B)
-Linolenic acid(D)
(A)Linoleic acid(B)Linolenic acid
(C)Arachidonic acid(D)Stearic acid
144.A
(A)Linoleic acid(B)
-Linolenic acid(D)
145.T
riglycerides are transported from liver to
(A)Chylomicrons(B)
(C)HDL
(D)LDL
(A)Chylomicrons(B)
(C)HDL
(D)LDL
(A)Chylomicrons(B)
(C)HDL
(D)LDL
(A)Alanine(B)
(C)Cysteine
(D)Proline
(A)Cysteine
161.An
MCQs IN BIOCHEMISTRY
(A)Galactose
(B)Sulphate
(C)Sphingosine(D)
(A)Ceramidase
(B)Sphingomyelinase
(C)Arylsulphatase A
(D)Hexosaminidase A
(A)Intestine(B)Adipose tissue
(C)Liver
(D)
(A)VLDL
(B)LDL
(C)HDL
(D)Chylomicrons
(A)Apo A specific(B)
Apo B-48 specific
(C)Apo C specific(D)Apo E specific
(A)Apo B-48 and Apo B 100
(B)Apo B-48 and Apo E
(C)Apo B-100 and Apo D
(D)Apo B-100 and apo D
(A)Apo A
(B)Apo C
(C)Apo E
(D)Apo C and Apo E
185.HDL is
(A)Adipose tissue(B)
(C)Intestine(D)
186.Na
(A)Chylomicrons
(B)VLDL
(C)LDL
(D)HDL of the hepatic origin
187.Heparin releasable hepatic lipase converts
(A)VLDL remnants into LDL
(B)Nascent HDL into HDL
(C)HDL
(D)HDL
(A)VLDL remnants into LDL
(B)Nascent HDL into HDL
(C)HDL
(D)HDL
(A)Liver(B)Kidney
(C)Intestine(D)Adipose tissue
(A)Hormone-sensitive lipase
(B)Glycerol kinase
(C)cAMP-dependent protein kinase
(D)Glycerol-3-phosphate dehydrogenase
198.A
MCQs IN BIOCHEMISTRY
Refsum’s disease results from a defect in
(A)Alpha-oxidation of fatty acids
(A)Hexose monophosphate shunt
(B)Oxidative decarboxylation of malate
(C)Extramitochondrial oxidation of isocitrate
(D)All of these
(A)Choline
MCQs IN BIOCHEMISTRY
Tangier disease are true except
(A)Citrate
(B)Isocitrate
259.De
(A)Synthesis occurs in cytosol and oxidation in
(B)Synthesis is decreased and oxidation
(C)NADH is required in synthesis and FAD in
(D)Malonyl CoA is formed during oxidation but
(A)Albumin(B)VLDL
(C)LDL
(D)HDL
(A)Fabry’s disease
(B)Krabbe’s disease
(C)Gaucher’s disease
MCQs IN BIOCHEMISTRY
(A)Groundnut oil(B)Soyabean oil
(C)Sunflower oil
(D)Safflower oil
(A)Egg
(B)Fish
(C)Milk
(D)
278.W
(A)Meat
(B)
(C)Butter
(D)Milk
279.W
(A)Egg yolk(B)Egg white
(C)Meat
(A)Milk
(B)
(C)Butter
(D)Cheese
(A)Cellulose(B)Pectin
(C)Inulin
(D)
(A)50%
(B)60%
(C)70%
(D)80%
(A)50%
(B)60%
(C)70%
(D)80%
284.A
(A)Haemolytic jaundice
(B)Hepatocellular jaundice
(C)Obstructive jaundice
(D)All of these
(A)2.0–3.6 gm/dl(B)2.0–3.6 mg/dl
(C)3.5–5.5 gm/dl(D)3.5–5.5 mg/dl
(A)2.0–3.6 mg/dl(B)2.0–3.6 gm/dl
(C)3.5–5.5 mg/dl(D)3.5–5.5 gm/dl
(A)Gilbert’s
disease(B)Haemolytic jaundice
(C)Viral hepatitis(D)
(A)Adipose tissue(B)
(C)Muscles(D)
(A)Haemolytic jaundice
(B)Hepatocellular jaundice
(C)Obstructive jaundice
(D)None of these
(A)Erythrocytes
MCQs IN BIOCHEMISTRY
(A)Glomerular filtration rate
(A)Saturated(B)Unsaturated
(C)Both (A) and (B)(D)None of these
(A)Gaucher’s disease
(B)Fabry’s disease
(C)Fabrile disease
(D)Niemann-Pick disease
(A)Serine
(B)Lysolecithin
(C)Sphingosine(D)
(A)1
(B)3
(C)4
(D)5
(A)Sphingosine(B)Iso-sphingosine
(C)Both (A) and (B)(D)None of these
(A)Sphingolipids(B)Sulpholipids
(C)Aminolipids(D)Glycolipids
Gaucher’s disease is characterized
(A)Lignoceric acid
(B)Nervonic acid
(C)Cerebomic acid
(D)Hydroxynervonic acid
(A)Brain
(B)Liver
(C)Kidney
(D)Muscle
(A)Hydrophilic(B)Hydrophobic
(C)Both (A) and (B)(D)None of these
(A)Increases
(B)Decreases
(C)Highly decreases
(D)Slightly and promptly decreases
(A)Electrophoresis
(B)Ultra centrifugation
(C)Centrifugation
(D)Immunoelectrophoresis
337.Very
-lipoproteins(B)
-lipoproteins(D)
MCQs IN BIOCHEMISTRY
Waxes contain higher alcohols named as
(A)Intestine(B)Muscle
(C)Kidney
(D)Liver
(A)Arachidonic acid(B)Oleic acid
MCQs IN BIOCHEMISTRY
383.Acr
olein Test is positive for
(A)Glycerol(B)
(C)Carbohydra
tes(D)Proteins
(A)Degree of unsaturation
(B)Saponification number
(C)Acid number
(A)Glycerol, fatty acids, phosphoric acid and
(B)Glycerol, sphingosine, choline and fatty acids
(C)Sphingosine, phosphoric acid, Glycerol and
(D)Sphingosine, fatty acids, phosphoric acid and
(A)Fabry’s disease
(B)Niemann pick disease
(C)Gaucher’s disease
(D)Tay-sach’s disease
(A)Glycerol, fatty acids, phosphoric acid, choline
(B)Glycerol, fatty acids, phosphoric acid
(C)Glycerol, fatty acids, phosphoric acid,
(D)Sphingol, fatty acids, phosphoric acid
(A)1
(B)2
(C)3
(D)4
(A)Sphingosine, fatty acids, glycerol and
(B)Sphingosine, fatty acids, galactose
(C)Glycerol, fatty acids, galactose
(D)Glycerol, fatty acids, galactose, sphingol
MCQs IN BIOCHEMISTRY
419.The ‘free
fatty acids’ (FFA) of plasma:
434.LCAT is
(A)Lactose choline alamine transferse
(B)Lecithin cholesterol acyl transferase
(C)Lecithin carnitine acyl transferase
(D)Lanoleate carbamoyl acyl transferase
(A)27
(B)21
(C)15
(D)12
436.A
(A)Mevalonate(B)
(C)Squalene(D)
MCQs IN BIOCHEMISTRY
(A)protein
(B)glycogen
(C)fatty acid outside the mitochondria
(D)fatty acid in the mitochondria
450.1
ATP (as high energy bonds):
(A)129(B)154
(C)83(D)25
MCQs IN BIOCHEMISTRY
480.A m
(A)They usually associate by covalent interactions
(B)They are structurally components of
(C)They are an intracellular energy source
(D)They are poorly soluble in H
MCQs IN BIOCHEMISTRY
(A)Fructose
(B)Glucose
(C)Sucrose(D)
(A)Vitamin B
(B)Tocopherols
(C)Folic acid
(D)Vitmain B
(A)2.5–4
(B)3.5–5
(C)4 to 5
(D)5–7
(A)Liver
(B)
(C)Pancreas(D)In
MCQs IN BIOCHEMISTRY
(A)Oleic acid(B)Linoleic acid
(C)Arachidonic acid(D)Linolenic acid
(A)6.0 Kcal/g(B)9.0 Kcal/g
(C)15.0 Kcal/g(D)12.0 Kcal/g
(A)2
(B)3
(C)4
(D)5
(A)Mepacrine(B)
(C)Glucocorticoids(D)
Selwanof’s test is positive in
(A)Glucose
(B)Fructose
(C)Galactose(D)Mannose
1. A2. A3. C4. C5. D6. A
7. C8. D9. D10. B11. D12. A
13. B14. A15. D16. B17. B18. D
19. C20. D21. C22. A23. D24. C
25. A26. A27. C28. B29. B30. D
31. A32. A33. C34. A35. A36. C
37. D38. A39. B40. C41. D42. A
43. B44. C45. D46. A47. D48. B
49. C50. C51. A52. B53. D54. B
55. C56. D57. A58. B59. D60. C
61. A62. A63. A64. D65. B66. A
67. A68. B69. A70. A71. A72. B
73. A74. D75. B76. A77. B78. A
79. B80. C81. C82. A83. A84. A
85. B86. B87. A88. B89. D90. C
91. D92. B93. A94. D95. B96. A
97. B98. D99. A100. A101. C102. B
103. A104. B
105. C106. C
107. B108. A
109. B110. C
111. D112. A
113. A114. A
115. D116. A
C120. D
121. D122. A
123. A124. D
125. B126. A
127. B128. A
129. B130. C
131. B132. C
133. C134. B
135. D136. A
137. C138. C
139. C140. B
C144. D
145. B146. D
147. C148. B
149. A150. A
151. A152. A
153. C154. B
155. D156. D
157. D158. D
159. D160. C
161. B162. B
163. D164. C
165. D166. B
167. D168. B
169. C170. A
171. D
173. A174. B
175. B176. C
177. D178. B
179. B180. C
181. C182. B
183. C184. D
185. D186. D
187. C188. B
189. D190. B
191. C192. D
193. C194. C
195. A196. D
197. B198. D
199. A200. C
C204. B
205. D206. A
207. D208. A
209. C210. C
211. B212. A
213. C214. D
215. D216. C
217. C218. D
219. A220. C
221. D222. C
223. D224. D
225. B
227. D228. A
229. D230. B
231. A232. A
233. D234. B
235. C236. C
237. D238. C
239. B240. D
241. B242. D
245. C246. A
MCQs IN BIOCHEMISTRY
247. C248. C
249. A250. A
251. C252. A
253. A254. B
255. C256. A
257. C258. A
259. A260. A
261. B262. A
263. C264. A
265. D266. A
267. D268. C
269. C270. C
271. A272. C
273. C274. A
275. A276. A
277. D278. C
279. A280. A
281. D282. C
283. B284. C
285. A286. C
287. A288. C
289. A290. D
293. C294. B
295. C296. B
297. B298. C
299. B300. A
301. B302. C
303. B304. C
305. C306. A
307. A308. B
309. D310. D
311. D312. A
313. C314. A
315. D
317. C318. B
319. D320. A
321. B322. C
323. D324. C
325. B326. A
327. B328. C
329. B330. C
331. A332. C
333. A334. A
335. A336. D
337. B338. A
339. A340. B
341. C342. C
343. A344. D
347. A348. C
349. D350. B
351. A352. B
353. D354. B
355. C356. C
C360. B
361. A362. C
363. D364. B
365. A366. D
367. A368. D
369. C370. D
371. C372. D
373. B374. B
375. D
377. A378. C
379. A380. B
381. D382. B
383. A384. A
385. A386. A
387. A388. C
389. B390. B
391. B392. D
393. C394. D
395. C396. B
397. D398. C
399. A400. C
401. B402. D
403. C404. B
405. D406. B
407. C408. D
409. C410. C
413. B414. D
415. A416. D
D420. B
421. A422. C
423. B424. C
425. B426. A
427. C428. B
D432. B
433. C434. B
435. A436. C
437. A438. C
439. C440. B
443. B444. A
445. D446. B
447. D448. B
449. C450. A
451. A452. B
455. C456. A
457. B458. C
461. D462. B
463. C464. B
465. A466. D
467. A468. A
469. B470. D
471. B472. D
473. B474. D
475. D476. B
479. A480. D
481. B482. B
483. D484. A
485. C486. D
487. B488. B
489. A490. B
491. C492. B
493. A494. A
495. D496. D
497. C498. C
499. B500. D
501. A502. D
503. D504. A
505. C506. B
507. B508. D
509. D510. D
511. D512. A
513. A514. A
515. D516. D
517. C518. A
519. B520. C
521. B522. A
523. C524. B
D528. C
529. B530. B
531. D
533. B534. A
535. D536. B
537. C538. D
539. B540. D
541. D542. B
543. A544. C
545. D546. C
547. D548. A
549. B
551. B552. B
553. D554. D
555. B556. B
MCQs IN BIOCHEMISTRY
EXPLANATIONS FOR THE ANSWERS
5. DThe fatty acids that cannot be synthesized by
VITAMINS
1.Vitamins are
(A)Accessory food factors
(B)Generally synthesized in the body
(C)Produced in endocrine glands
(D)Proteins in nature
CHAPTER 5
CHAPTER 5
CHAPTER 5
CHAPTER 5
VV
VV
ITIT
ITIT
AMINSAMINS
AMINSAMINS
MCQs IN BIOCHEMISTRY
11.The normal serum concentration of
(A)5–10(B)15–60
(C)100–150(D)0–5
12.One manifestation of vitamin A deficiency
(A)Painful joints
(B)Night blindness
(C)Loss of hair
(D)Thickening of long bones
13.Deficiency of Vitamin A causes
(A)Xeropthalmia
(B)Hypoprothrombinemia
(C)Megaloblastic anemia
(D)Pernicious anemia
14.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
VITAMINS
29.The
ββ
ββ
(A)Infrared light
(B)Dim light
MCQs IN BIOCHEMISTRY
47.In the individuals who are given liberal
(A)1–1.4
(B)2–4
(C)1–10
(D)10–20
48.The vitamin which would most likely
VITAMINS
65.Riboflavin deficiency causes
(A)Cheilosis
(B)Loss of weight
MCQs IN BIOCHEMISTRY
85.Deficiency of vitamin B
(A)Obese person(B)Thin person
(C)Alcoholics(D)Di
VITAMINS
102.Vi
MCQs IN BIOCHEMISTRY
(A)Sulphydryl gr
oup(B)Carboxyl group
(C)Amide group(D)All of these
(A)Glycolysis(B)
(C)HMP shunt(D)
(A)Malate dehydrogenase
(B)Succinate dehydrogenase
(C)Glucose-6-phosphate dehydrogenase
(D)HMG CoA reductae
(A)Citric acid cycle
(B)HMP shunt
(D)Both (A) and (C)
124.Niacin can be
(A)Histidine(B)Pheny
(C)Tyrosine(D)Tr
125.Da
(A)5 mg
(B)10 mg
(C)20 mg
(D)30 mg
(A)Wheat
(B)Polished rice
(C)Maize and /or sorghum
(D)None of these
127.In
(A)Exposed parts of body
(B)Covered parts of body
(C)Trunk only
(D)All parts of the body
128.Niacin d
(A)Hartnup disease(B)
VITAMINS
139.Pyri
MCQs IN BIOCHEMISTRY
156.Vitamin B
(A)Albumin(B)T
ranscortin
(C)Transcobalamin I(D)Transcobalamin II
(A)Bacteria only
(B)Plants only
(C)Animals only(D)
158.Deficiency of vitamin B
(A)Decreased intake of vitamin B
(B)Atrophy of gastric mucosa
(C)Intestinal malabsorption
(D)All of these
159.Deficiency of vitamin B
(A)Carr-Price reaction
(B)Ames assay
(C)Watson-Schwartz test
(D)Schilling test
(A)Days
(B)Weeks
(C)Months(D)Y
(A)Collagen(B)Bile acids
(C)Bile pigments(D)Epinephrine
(A)Potassium(B)Iodine
(C)Iron
(D)
(A)D-Ascorbic acid
(B)D-Dehydroascorbic acid
(C)L-Ascorbic acid
(D)Both A and B
(A)Bile acids from cholesterol
(B)Bile salts from bile acids
(C)Vitamin D from cholesterol
(D)All of these
(A)Beriberi
(B)Pellagra
(C)Pernicious anaemia
(D)Scurvy
166.An
(A)Measuring plasma ascorbic acid
(B)Measuring urinary ascorbic acid
(C)Ascorbic acid saturation test
(D)All of these
167.Da
(A)100 mg(B)25 mg
(C)70 mg
(D)100 mg
(A)Thiamin
(B)Ribovflavin
(C)Pyridoxine(D)
(A)Thiamin(B)Pyridoxine
(C)Folic acid
(D)Cyanocobalamin
170.A v
(A)Thiamin(B)Niacin
(C)Folic acid
(D)Cyanocobalamin
VITAMINS
174.Two molecules of vitamin A can be formed
-Carotene(B)
-Carotene(D)All
ββ
ββ
MCQs IN BIOCHEMISTRY
VITAMINS
210.A
(A)Phylloquinone(B)Farnoquinone
(C)Menadione(D)None of these
(A)Vitamin K deficiency
(B)Liver damage
(C)Both (A) and (B)
(D)None of these
212.A
MCQs IN BIOCHEMISTRY
(A)Mitochondria
(B)Microsomes
(C)Both (A) and (B)(D)None of these
231.Vi
(A)Superoxide(B)Peroxide
(C)Trioxide(D)
(A)Vitamin A(B)Vitamin D
(C)Vitamin K(D)Vitamin C
(A)Muscles(B)Nerves
(C)Gonads(D)All of these
234.Vitamin K
(A)VII(B)IX
(C)X(D)All of these
(A)2, 4-dinitro benzene
(B)2, 6-Dichlorophenol Indophenol
(C)2, 4-dibromobenzene
(D)2, 6-dibromo benzene
(A)Vitamin A(B)Vitamin B
(C)Vitamin C
(D)Vitamin D
(A)Poor healing of wounds
VITAMINS
249.A
(A)Absorbed in the intestines
MCQs IN BIOCHEMISTRY
(A)Liver
(B)Kidneys
(C)Inte
stine(D)
(A)Cytochrome -
a(B)Parathyroid hormone
Cytochrome-b(D)
(A)Biotin
(B)A
(C)Albumin(D)Calcium salts
(A)Vitamin B
(B)Adenyl cobamide
(C)Benzimidazole cobamide
VITAMINS
(A)Vitamin B
(B)Glycoprotein
(C)R-Proteins(D)
(A)Prolonged(B)Dangerous
(C)Intermittent(D)Idiopathic
MCQs IN BIOCHEMISTRY
307.In
VITAMINS
(A)Protein
(B)Iodine
(C)Carbohydrate(D)Lipid
327.A
(A)Cheliosis(B)Beriberi
(C)Pernicious anemia(D)
Scurvy
328.In
(A)Night blindness
(B)Osteomalacia
MCQs IN BIOCHEMISTRY
(A)Biotin
(B)
Avidin
(C)Albumin(D)Calcium salts
(A)Vitamin B
(B)Adenyl cobamide
(C)Benzimidazole cobamide
VITAMINS
(A)Vitamin A(B)Vitamin D
(C)Vitamin E(D)Vitamin K
(A)Ariboflavinosis
(B)Deficiency of Vitamin C
(C)Deficiency of Vitamin B
(D)Deficiency of folate
368.One of the main f
(A)Carboxylase for the formation of
MCQs IN BIOCHEMISTRY
385.An
(A)Aminopterin(B)Dicoumarol
(C)Pyrithiamine
(D)Isoniazid
(A)Water-soluble vitamin
(B)Fat soluble vitamin
(C)Purine base
(D)Pyrimidine base
(A)Aminopterin(B)Dicoumarol
(C)INH
(D)Sulphanomides
(A)Thiamine
(B)Riboflavin
(C)Niacin
(D)Pyridoxine
389.T
(A)Pernicious anemia(B)
(C)Pellegra(D)
(A)Thiamine, Niacin and Riboflavin
(B)Thiamin, Folic acid, Choline
(C)Thiamine, Riboflavin, Pantothenic acid
(D)Thiamine, Pyridoxin, Vitamin B
(A)Rice
(B)Milk
(C)Egg
(D)Lemon
(A)Nicotinamide
(B)Pyridoxine
(C)Thiamine
(D)Riboflavin
VITAMINS
MCQs IN BIOCHEMISTRY
(A)Soyabean(B)
(C)Alfa alfa(D)Oysters
VITAMINS
2. B
8. A
10. A
11. B
12. B
14. D
15. B
21. B
22. D
31. D
37. C
38. B
39. A
40. D
41. D
42. D
45. B
51. D
55. D
56. B
60. D
62. B
63. B
69. D
74. B
79. C
81. A
82. D
83. C
84. A
89. D
93. D
98. D
99. C100. B
101. B102. B
103. D104. C
105. C106. B
107. C108. D
109. A110. D
111. A112. D
113. B114. D
115. A116. D
117. D118. C
119. C120. B
121. C122. A
123. D124. D
125. C126. C
127. A128. A
129. C130. D
131. A132. A
133. D134. C
135. D136. D
137. B138. C
139. C140. B
141. B142. B
143. D144. D
145. C146. D
147. D148. B
149. D150. A
151. C152. D
153. B154. D
155. C156. D
157. A158. D
159. D160. D
161. C162. C
163. C164. A
165. D166. C
167. C168. D
169. A170. B
173. D174. B
175. D176. B
177. D178. B
179. A180. A
181. D182. D
183. B184. A
185. B186. C
187. D188. C
189. D190. C
191. C192. B
193. C194. D
195. D196. C
197. B198. B
199. B200. C
203. A204. C
205. A206. C
207. D208. D
209. B210. C
211. C212. A
213. C214. D
215. A216. D
217. D218. C
219. D220. D
221. A222. D
223. B224. D
225. D226. C
227. A228. A
229. B230. C
231. B232. A
233. D234. D
235. B236. C
C240. B
241. B242. B
243. C244. C
245. A246. C
MCQs IN BIOCHEMISTRY
247. D248. A
249. B250. C
251. D252. C
253. B254. D
255. C256. B
257. C258. C
259. A260. B
261. D262. D
263. B264. A
265. C266. D
267. B268. A
269. B270. B
271. A272. D
C276. D
277. A278. C
279. A280. D
281. D282. B
283. B284. A
285. D286. B
287. B288. A
289. B290. B
291. A292. B
293. A294. A
295. B296. C
297. B298. A
299. C300. C
301. A302. B
303. B304. A
305. D306. D
307. C308. C
309. C310. B
311. C312. A
313. D314. D
315. A316. A
317. D318. D
319. B320. D
321. C322. C
323. C324. B
325. A326. C
D330. C
331. B332. A
333. B334. B
335. A336. D
337. D338. B
339. A340. D
341. D342. B
343. A344. B
345. B346. A
347. D348. A
349. D350. C
351. D352. A
353. A354. B
355. D356. B
357. C358. A
359. D360. B
361. B362. A
363. B364. B
365. A366. B
367. A368. A
369. B370. C
371. B372. A
375. A376. B
377. B378. B
379. A380. C
C384. C
385. A386. D
387. D388. A
389. A390. D
391. D392. B
393. D394. A
395. C396. B
397. A398. D
401. B402. C
403. B404. B
405. A406. B
407. D408. D
409. C410. A
411. B412. C
413. B414. A
415. C416. D
417. A418. C
419. D420. D
421. A422. D
C426. B
427. C428. A
429. A430. C
VITAMINS
7. DThe four fat soluble vitamins (A, D, E, K) are
intentionally left
blank
1.The compound which has the lowest
(A)Chylomicron(B)
-Lipoprotein(D)
2.Non steroidal anti inflammatory drugs,
(A)Lipoxygenase(B)
(C)Phospholipase A
(D)Lipoprotein lipase
3.From arachidonate, synthesis of prostag-
(A)Cyclooxygenase
(B)Lipoxygenase
(C)Thromboxane synthase
(D)Isomerase
4.A Holoenzyme is
(A)Functional unit
(B)Apo enzyme
(C)Coenzyme(D)
5.Gaucher’s disease is due to the deficiency
-Fucosidase(B)
-Glucosidase(D)Sphingomyelinase
6.Neimann-Pick disease is due to the defi-
(A)Hexosaminidase A and B
(B)Ceramidase
(C)Ceramide lactosidase
(D)Sphingomyelinase
CHAPTER 6
CHAPTER 6
CHAPTER 6
CHAPTER 6
EE
EE
NZYMESNZYMES
NZYMESNZYMES
7.Krabbe’s disease is due to the deficiency
(A)Ceramide lactosidase
(B)Ceramidase
(D)GM1
8.Fabry’s disease is due to the deficiency of
(A)Ceramide trihexosidase
(B)Galactocerebrosidase
(C)Phytanic acid oxidase
(D)Sphingomyelinase
9.Farber’s disease is due to the deficiency
(B)Ceramidase
(D)Arylsulphatase A.
MCQs IN BIOCHEMISTRY
11.Example of an extracellular enzyme is
(A)Lactate dehydrogenase
(B)Cytochrome oxidase
(C)Pancreatic lipase
(D)Hexokinase
12.Enzymes, which are produced in inactive
(A)Papain(B)L
(C)Apoenzymes(D)Proenzymes
13.An example of ligases is
(A)Succinate thiokinase
(B)Alanine racemase
(C)Fumarase
(D)Aldolase
14An example of lyases is
MCQs IN BIOCHEMISTRY
40.Cocarboxylase is
(A)Thiamine pyrophosphate
(B)Pyridoxal phosphate
(C)Biotin
(D)CoA
41.A coenzyme containing non aromatic
57.The isoenzymes LDH
(A)Myocardial infarction
(B)Peptic ulcer
(C)Liver disease
(D)Infectious diseases
MCQs IN BIOCHEMISTRY
76.Glucose absorption is promoted by
(A)Vitamin A
(B)Thiamin
(C)Vitamin C(D)Vitamin K
77.The harmone acting directly on intestinal
(A)Insulin
(B)
(C)Thyroxine(D)V
asopressin
78.Given that the standard free energy
∆∆
∆∆
G°) for the hydrolysis of ATP is
∆∆
∆∆
glucose is Glucose + ATP
oo
oo
Phosphate + ADP.
(A)–10.6 Kcal/mol(B)–7.3 Kcal/mol
(C)–4.0 Kcal/mol(D)+4.0 Kcal/mol
79.At low blood glucose concentration, brain
(A)Low K
(B)Low K
(C)Specificity of glucokinase
(D)Blood brain barrier
80.In the reaction below, Nu TP stands for
oo
oo
+ NuDP.
(A)ATP
(B)CTP
(C)GTP
(D)UTP
81.In the figures shown below, fructose 1,6-
(A)A
(B)B
(C)C
(D)D
82.The enzyme of the glycolic pathway,
(A)Hexokinase(B)
(C)Enolase(D)
90.Phosphofructokinase key enzyme in
(A)Citrate and ATP(B)AMP
(C)ADP(D)TMP
91.One of the enzymes regulating glycolysis
(A)Phosphofructokinase
(B)Glyceraldehyde-3-phosphate dehydrogenase
(C)Phosphotriose isomerase
(D)Phosphohexose isomerase
92.Hexokinase is inhibited in an allosteric
(A)Glucose-6-Phosphate
(B)Glucose-1-Phosphate
(C)Fructose-6-phosphate
(D)Fructose-1, 6-biphosphate
93.A reaction which may be considered an
(A)Glucose 6-Phosphate
(B)3-Phosphoglycerate
(C)2-phosphoglycerate
(D)Pyruvate
MCQs IN BIOCHEMISTRY
αα
αα
(C)Malate
-Succinate
110.
(C)Citrate
(D)Succinate
αα
αα
(B)
(C)Malate
117.
The coenzyme not involved in the
(A)Aconitase
(B)Fumarase
(C)Fumarase
(D)Malate dehydrogenase
121.In
MCQs IN BIOCHEMISTRY
(A)Branching enzyme
(B)Debranching enzyme
(C)Glycogen synthase
(D)Phosphorylase
136.Mc Ar
dle’s syndrome is characterized by
(A)Liver phosphorylase
(B)Muscle phosphorylase
(C)Branching enzyme
(D)Debranching enzyme
Pompe’s disease is caused due to
(A)Lysosomal
(B)Glucose-6-phosphatase
(C)Glycogen synthase
(D)Phosphofructokinase
(A)Debranching enzyme
(B)Branching enzyme
(C)Acid maltase
(D)Glucose-6-phosphatase
139.Her’s
(A)Muscle phosphorylase
(B)Liver phosphorylase
(C)Debranching enzyme
(D)Glycogen synthase
140.Tarui
(A)Liver phosphorylase
(B)Muscle phosphorylase
(C)Muscle and erythrocyte phosphofructokinase
(D)Lysosomal acid maltase
(A)Maltase dehydrogenase
(B)Hexokinase
pentose phosphate pathway, the
(A)Glucose-6-phosphate dehydrogenase
(B)Aldolase
(C)Fructose 1, 6-bisphosphatase
(D)Phosphohexose isomerase
(A)Liver and kidney
(B)Skin and pancreas
(C)Lung and brain
(D)Intestine and lens of eye
151.An
(A)Pyruvate kinase
(B)Pyruvate carboxylase
(C)Hexokinase
(D)Phosphohexose isomerase
(A)Cytosol
(B)
(C)Nucleus(D)Golgi bodies
MCQs IN BIOCHEMISTRY
165Conversion of fructose to sorbitol is
(A)Sorbitol dehydrogenase
(B)Aldose reductase
(C)Fructokinase
(D)Hexokinase
166.A
(A)K
for fructose is very high
(B)K
for fructose is very low
(C)Activity is affected by fasting
(D)Activity is affected by insulin
∆∆
∆∆
MCQs IN BIOCHEMISTRY
197.In
(C)Formed from gluconeogenesis
(D)Formed from glycogenolysis
213.In the biosynthesis of
(A)2-Monoacylglycerol
(B)1, 2-Diacylglycerol
(C)Lysophosphatidic acid
(D)Phosphatidic acid
214.The
(A)Liver(B)Kidney
(C)Intestine(D)Adipose tissue
(A)1, 2-Diacylglycerol phosphate
(B)1-Acylglycerol 3-phosphate
(C)Glycerol 3-phosphate
MCQs IN BIOCHEMISTRY
(A)Fatty acids(B)
(C)Phospholipids(D)T
230.A
(A)Choline(B)
(C)Calcium(D)Vitamin C
(A)CH
Cl
(B)CCl
(C)Na
(D)Riboflavin
(A)Mitochondria
(B)Golgi apparatus
(C)Nucleus
(A)Insulin
(B)
(C)Epinephrine(D)
MCQs IN BIOCHEMISTRY
261.An
important finding in Tay-sach’s disease is
(A)Renal failure
(B)Accumulation of gangliosides in brain and
(C)Cardiac failure
(D)Anemia
The enzyme deficient in Krabbe’s disease is
Hexosaminidase A(B)Ar
-Galactosidase(D)
(A)Farber’s disease(B)Fabry’s disease
(C)Sandhoff’s disease
(D)Refsum’s disease
(A)Ceramidase
(B)Glucocerebrosidase
(C)Galactocerebrosidase
(D)Sphingomyelinase
265.W
olman’s disease is
(A)Cholesteryl ester hydrolase
(B)Hexosaminidase A
(D)Arylsulphatase A
266.The enzyme deficient in Sandhoff’s disease
(B)Hexosaminidase A and B
(A)Pyruvate carboxylase
(A)Phenylalanine hydroxylase
(B)Tyrosinase
(C)p-Hydroxyphenylpyruvic acid oxidase
(D)Tyrosine dehydrogenase
(A)p-Hydroxyphenylpyruvate hydroxylase
MCQs IN BIOCHEMISTRY
294.An
(A)Initial substrate of the pathway
(B)Substrate analogues
(C)Product of the reaction catalysed by allosteric
(D)Product of the pathway
295.When the velocity of an enzymatic reaction
(A)Half of K
(B)Equal to K
(C)Twice the K
(D)Far above the K
296.In Lineweaver-Burk plot, the y-inte
(A)V
(B)K
(C)K
(D)1/K
297.In
311.Allo
(A)Feedback inhibition
MCQs IN BIOCHEMISTRY
328.V
(A)pH
(B)Temperature
(A)Covalent modification
(B)Allosteric regulation
(C)Both (A) and (B)
(D)None of these
344.An alloste
MCQs IN BIOCHEMISTRY
(A)Glucokinase
(B)Hexokinase
(C)Phosphohexose isomerase
(D)None of these
363.ATP is a co-substrate as well as an allos-
(A)Phosphofructokinase
(B)Hexokinase
(C)Glucokinase
(D)None of these
(A)Glucose
(B)Glucose-6-phosphate
(C)Glucose-1-phosphate
(D)Maltose
380.A
(A)Amylopectin(B)dextrin
(C)Amylose(D)
(A)Liver
(B)Kidneys
(C)Muscles(D)
382.A
(A)NAD
(B)Pyridoxal phosphate
(C)Thiamin pyrophosphate
(D)Coenzyme A
383.If
(A)2 ATP equivalents(B)3 ATP equivalents
(C)4 ATP equivalents(D)8 ATP equivalents
384.A
(A)4 subunits(B)8 subunits
(C)12 subunits(D)16 subunits
(A)Catalytic subunits of protein kinase
(B)Regulatory subunits of protein kinase
(C)Catalytic subunits of phosphorylase kinase
(D)Regulatory subunits of phosphorylase kinase
(A)Myocardium(B)Kidneys
(C)Erythrocytes(D)Thrombocytes
(A)Phosphatidic acid(B)
(C)Glycerol
(D)Glucose
(A)Brain(B)Kidneys
(C)Muscles(D)
(A)Glycerol(B)
(C)Alanine(D)Leucine
(A)ATP
(B)ADP
(C)GTP
(D)GDP
(A)Streptokinase(B)
(C)Riboflavinase
(D)Both (A) and (B)
392.A
(A)Phosphofructokinase
(B)Pyruvate kinase
(C)Phosphoenol pyruvate carboxykinase
(D)Glucokinase
(A)Covalent modification
(B)Allosteric regulation
(C)Induction and repression
(D)All of these
(A)16 Carbon atoms(B)18 Carbon atoms
(C)20 Carbon atoms(D)24 Carbon atoms
(A)Breakdown of existing fatty acids
MCQs IN BIOCHEMISTRY
(A)Mitochondria(B)
(C)Microsomes(D)
ββ
ββ
(A)Insulin
(B)
(C)Prostaglandin E
(D)Ca
(A)Acidic
pH(B)
(C)Basic pH(D)Optimum pH
(A)Alkaline phosphatase
(B)Acid phosphatase
(C)Leucine aminopeptidase
(A)Intra molecular rearrangement
(B)Breaking of hydrogen bonds
(C)Covalent modification
(D)Polymerisation
(A)Lactate dehydrogenase
(B)Succinate dehydrogenase
(C)Malate dehydrogenase
(D)Pepsin
(A)Isomerase(B)Lyase
(C)Ligase
(D)Oxido reductase
(A)Oxidase
(B)Monooxygenase
(C)Dioxygenase
(D)Anaerotic dehydrogenase
__________ as a cofactor.
(A)NAD
only(B)NADP
(C)NAD
(D)FMN and FAD
(A)reaches a minimum, then increases
(B)reaches a maximum, then decreases
(C)increases
(D)decreases
422.A
(A)galactose-6-phosphate
(B)isocitric acid
(C)Glucose-1-phosphate
(D)Fructose 1, 6 diphosphate
αα
αα
MCQs IN BIOCHEMISTRY
(A)Urease
(B)Glutaminase
(C)Arginase(D)
(A)Lyase
(B)
(C)Isomerase(D)Hydrolase
432.V
(A)The molecular weight of the enzyme
(B)Km value
(C)Isoelectric pH
(D)Pk value
(A)Lysine
(B)Tyrosine
(C)Serine
(D)Histidine
(A)Postulates the formation of an enzyme
(B)Enables us to calculate the isoelectric point of
(C)States that the rate of a chemical reaction may
(D)States that the reaction rate is proportional to
Schardinger’s enzyme is
(A)Lactate dehydrogenase
(B)Xanthine dehydrogenase
(C)Uric oxidase
(D)L amino acid dehydrogenase
448.Tr
yptophan pyrolase is currently known
(A)Tryptophan deaminase
(B)Tryptophan dioxygenase
(C)Tryptophan mono oxygenase
(D)Tryptophan decarboxylase
449.An
(A)Amylase(B)L
(C)Trypsin
(D)
450.Tr
(A)Hemoglobin
(B)Albumin
(C)Histone(D)DNA
(A)Zymogens(B)Isoenzymes
(C)Proenzymes
(D)Pre-enzymes
452.In
MCQs IN BIOCHEMISTRY
460.In
(A)Inhibited enzyme
(B)Cooperative enzyme
(C)Allosteric enzyme(D)Constitutive enzyme
461.In
water may be added to a C—C double
(A)Hydrolase
(B)Hydratase
(C)Hydroxylase(D)
462.‘
(A)The active site is flexible and adjusts to
(B)The active site requires removal of PO
(C)The active site is complementary in shape to
(D)Substrates change conformation prior to active
463.In
MCQs IN BIOCHEMISTRY
(A)HI
(B)H
(C)(CH
CO(D)CH
491.A
506.An
(A)Lowering the energy of activation
(B)Causing the release of heat which acts as a
(C)Increasing molecular motion
MCQs IN BIOCHEMISTRY
(A)Pico seconds(B)Micro seconds
(C)Milli seconds(D)
523.An enzyme can accelerate a reaction up to
(A)10
times(B)10
(C)10
times(D)
524.In
(A)Flowers only(B)
(C)All living cells(D)Storage organs only
(A)Vitamin(B)
(C)Modulator(D)
MCQs IN BIOCHEMISTRY
(A)Fe
(B)Mo
(C)Zn
(D)Ca
(A)PEP carboxylase
(B)RuBP carboxylase
(C)Carbonic anyhdrase
(D)None of these
556.A
(A)Taq polymerase
(B)RNA polymerase
(C)Ribonuclease
(D)Endonuclease
571.Which of the following is a microsomal en-
MCQs IN BIOCHEMISTRY
1. A2. B3. A4. D5. C6. D
7. C8. A9. B10. D11. C12. D
13. A14. B15. D16. A17. B18. C
19. B20. D21. A22. A23. B24. B
25. D26. B27. A28. A29. A30. B
31. C32. A33. B34. C35. A36. B
37. A38. B39. D40. C41. D42. A
43. A44. B45. C46. A47. D48. B
49. C50. B51. B52. A53. A54. C
55. C56. D57. C58. C59. A60. B
61. A62. C63. A64. D65. A66. D
67. A68. C69. B70. B71. A72. B
73. A74. B75. A76. B77. C78. C
79. A80. A81. C82. C83. B84. D
85. B86. B87. D88. D89. D90. A
91. A92. A93. A94. B95. A96. B
97. A98. A99. A100. A101. A102. B
103. A104. C105. A106. D107. B108. A
109. D110. C111. B112. B113. D114. A
115. B116. A117. B118. C119. B120. C
121. A122. C123. C124. D125. A126. A
127. B128. B129. B130. B131. C132. A
133. D134. A135. B136. B137. A138. B
139. B140. C
141. D142. B143. A144. B
145. B146. A147. A148. C149. A150. A
151. B152. B153. D154. A155. A156. D
157. A158. A159. A160. A161. A162. A
163. B164. A165. A166. B167. B168. C
169. A170. D171. D172. A173. C174. B
175. B176. A177. C
179. D180. B
181. D182. B
183. D184. C
185. C186. A
187. D188. C
189. A
191. C192. C
193. A194. C
195. A196. A
197. B198. B
199. B200. A
201. D
D204. D
205. B206. A
207. D208. A
209. A210. D
211. A212. A
213. D214. D
215. A216. A
217. A218. A
219. D220. D
221. C222. C
223. B224. D
225. A226. A
227. B228. B
229. D230. A
231. B232. D
233. A234. A
235. D236. B
237. A
239. B240. C
241. B242. A
243. B244. A
245. A246. A
247. A248. A
249. A250. C
251. B252. C
253. B254. D
255. C256. D
257. A258. B
259. D260. C
261. B262. C
263. A264. D
265. A266. B
267. C268. A
269. B270. C
271. C272. A
273. D
275. B276. C
277. B278. C
C282. B
283. B284. D
285. C286. D
287. C288. A
289. C290. D
291. C292. B
293. C294. D
295. D296. B
297. D298. C
299. B300. B
301. B302. D
303. D304. A
305. B306. D
307. C308. B
311. A312. C
313. D314. B
317. C318. B
319. B320. A
321. D322. A
323. A324. B
325. C326. C
329. B330. A
331. C332. C
335. D336. A
337. A338. D
339. C340. D
341. C342. C
343. C344. A
345. D
347. C348. C
349. C350. C
351. C352. C
353. C354. B
355. C356. A
357. C358. A
359. D360. D
361. D362. B
363. A364. D
365. C366. A
367. D368. A
C372. B
373. C374. A
375. C376. A
377. B378. B
379. C380. B
383. B384. D
385. B386. C
387. D388. C
389. D390. C
391. D392. C
393. C394. A
395. D396. D
397. C398. C
D402. B
403. C404. B
405. D406. D
407. A408. C
409. C410. D
411. B412. B
413. B414. D
415. A416. C
417. D418. D
419. C420. C
421. B422. D
423. A424. B
425. D426. B
427. B428. D
429. D430. C
431. D432. B
433. C434. A
435. D
437. A438. B
439. D440. B
441. A
443. B444. C
445. A446. A
447. B448. B
449. B450. D
451. B452. C
455. D456. A
457. D458. B
459. C460. D
461. B462. C
463. B464. D
465. B466. D
467. D468. D
469. C470. B
D474. C
475. D476. D
477. B478. B
479. D480. A
481. D482. B
485. C486. C
487. A488. A
489. B490. A
491. A492. D
493. C494. B
497. A498. D
499. D500. D
501. D502. C
503. C504. A
505. C506. A
507. B508. B
509. B510. A
MCQs IN BIOCHEMISTRY
511. B512. C
513. A514. D
515. A516. A
517. C518. C
C522. C
523. A524. C
525. B526. B
527. A528. A
529. D530. A
531. D532. D
533. B534. A
535. D536. C
537. A538. D
539. B540. A
541. A542. B
543. C544. A
545. D546. D
547. C548. A
551. C552. A
553. C554. A
555. B556. B
557. C558. B
559. C560. A
561. D
563. B564. B
565. B566. D
567. A568. A
569. C570. D
571. D572. A
573. C
575. A576. C
577. D578. C
579. B580. B
581. B582. B
583. B584. B
585. C586. B
EXPLANATIONS FOR THE ANSWERS
4. DThe functional unit of an enzyme is referred to
47. DConcentration of enzyme, concentration of
factors that influence enzyme activity.
89. DIt is a straight line graphic representation
intentionally left
blank
1.When ATP forms AMP
(A)Inorganic pyrophosphate is produced
(B)Inorganic phosphorous is produced
(C)Phsophagen is produced
(D)No energy is produced
2.Standard free energy (
∆∆
∆∆
of ATP to ADP + Pi is
(A)–49.3 KJ/mol(B)–4.93 KJ/mol
(C)–30.5 KJ/mol(D)–20.9 KJ/mol
3.Standard free energy (
∆∆
∆∆
(A)–43.3 KJ/mol(B)–30.5 KJ/mol
(C)–27.6 KJ/mol(D)–15.9 KJ/mol
4.Standard free energy (
∆∆
∆∆
(A)–61.9 KJ/mol(B)–43.1 KJ/mol
(C)–14.2 KJ/mol(D)–9.2 KJ/mol
5.Standard free energy (
∆∆
∆∆
(A)-–51.4 KJ/mol(B)–43.1 KJ/mol
(C)–30.5 KJ/mol(D)–15.9 KJ/mol
6.The oxidation-reduction system having
(A)Ubiquinone ox/red
(B)Fe
(C)Fe
(D)NAD
CHAPTER 7
CHAPTER 7
CHAPTER 7
CHAPTER 7
MM
MM
INERALINERAL
INERALINERAL


MM
MM
7.If
∆∆
∆∆
ABC
10moles10moles10moles
(A)–4.6 RT(B)–2.3 RT
(C)+2.3 RT(D)+4.6 RT
8.Redox potential (E
(A)–0.67(B)–0.32
(C)–0.12(D)
9.Redox potential (E
(A)+0.03(B)+0.08
(C)+0.10(D)+0.29
10.Redox potential (E
(A)–0.29
(B)–0.27
(C)–0.08
(D)
MCQs IN BIOCHEMISTRY
13.A molybdenum containing oxidase is
(A)Cytochrome oxidase
(B)Xanthine oxidase
(C)Glucose oxidase
(D)L-Amino acid oxidase
14.A copper containing oxidase is
(A)Cytochrome oxidase
(B)Flavin mononucleotide
(C)Flavin adenine dinucleotide
(D)Xanthine oxidase
15.The mitochondrial superoxide dismutase
(A)Mg
(B)Mn
(C)Co
(D)Zn
16.Cytosolic superoxide dismutase contains
(A)Cu
(B)Mn
(C)Mn
(D)Cu
17.Cytochrome oxidase contains
(A)Cu
(B)Cu
(C)Cu
(D)Cu
18.Characteristic absorption bands exhibited
band(B)
bands(D)
19.Monooxygenases are found in
(A)Cytosol
(B)
(C)Mitochondira
(D)Microsomes
20.A component of the respiratory chain in
(A)Coenzyme Q
(B)Coenzyme A
29.One of the site of phsosphorylation in
MCQs IN BIOCHEMISTRY
44.In mammalian liver the rate controlling
(A)ALA synthase
(B)ALA hydratase
(C)Uroporphyrinogen I synthase
(D)Uroporphyrinogen III cosynthase
45.The condensation of 2 molecules of
δδ
δδ
(A)ALA synthase
(B)ALA hydratase
(C)Uroporphyrinogen synthase I
(D)Uroporphyrinogen synthase III
46.The enzyme
δδ
δδ
(A)Zinc
(B)
(C)Magnesium(D)
47.A cofactor required for the activity of the
(A)Cu
(B)Mn
(C)Mg
(D)Fe
48.The number of molecules of porphobili-
59.The characteristic urinary finding in por-
(A)Increased quantity of porphobilinogen
(B)Increased quantity of red cell protoporphyrin
(C)Increased quantity of uroporphyrin
(D)Increased quantity of
60.Hereditary coproporphyria is caused due
(A)Protoporphyrinogen oxidase
(B)ALA synthase
(C)ALA dehydratase
(D)Coproporphyrinogen oxidase
61.The enzyme involved in variegate por-
(A)Protoporphyrinogen oxidase
(B)Coproporphyrinogen oxidase
(C)Uroporphyrinogen decarboxylase
(D)ALA decarboxylase
62.Protoporphyria (erythrohepatic) is char-
(A)ALA synthase
(B)ALA hydratase
(C)Protophyrinogen oxidae
(D)Ferrochelatase
MCQs IN BIOCHEMISTRY
96.The half life of Ig M is
(A)2 days
(B)4 days
(C)5 days
(D)8 days
97.The normal serum level of Ig M is
(A)50 mg%(B)120 mg%
(C)200 mg%(D)300 mg%
98.The immunoglobulin associated with
(A)Ig E
(B)Ig D
(C)Ig M
(D)Ig A
99.The immunoglobulin having least concen-
(A)Ig A
(B)Ig M
(C)Ig D
(D)Ig E
(A)1–6 days(B)2–8 days
(C)10 days(D)20 days
(A)Ig D
(B)Ig E
(C)Ig A
(D)Ig G
(A)6 days
(B)2–4 days
(C)5–10 days(D)12–20 days
(A)100 mg%(B)200 mg%
(C)300 mg%(D)400 mg%
MCQs IN BIOCHEMISTRY
(A)120–140
(B)200–300
(C)120–140
(D)200–300
116.In i
(A)The plasma bound iron is low
(B)The plasma bound iron is high
(C)Total iron binding capacity is low
(D)Both the plasma bound iron and total iron
(A)400–500 mg(B)1–2 g
(C)2–3 g
(D)4–5 g
118.In
(A)Both the bound iron and total iron binding
(B)Both the bound iron and total iron binding
(C)Only bound iron may be high
(D)Only the total iron binding capacity may be
(A)5 mg
(B)8 mg
(C)10 mg
(D)15 mg
(A)10–20
(B)20–30
(C)30–40
(D)60–70
121.A
(A)Iron responsive
(B)Pyridoxine responsive
(C)Vitamin B
(D)Folate responsive
122.A
(A)Spinach
(B)Milk
(C)Tomato(D)Potato
(A)Organ meats(B)
(C)Tomato(D)Potato
124.An
(A)Fe deficiency anemia
(B)Sideroblastic anemia
(C)Folate deficiency anemia
(D)Sickle cell anemia
(A)Iron deficiency anemia
(B)Pregnancy
(C)Spherocytosis
(D)Sickle cell anemia
(A)Stomach and duodenum
(B)Ileum
(C)Caecum
(D)Colon
(A)Hemosiderin(B)
(C)Cytochrome C
(D)Peroxidase
(A)Stored primarily in the spleen
(A)10 mg
(B)30 mg
(C)64 mg
(D)100 mg
(A)5 mg
(B)10 mg
(C)15 mg
(D)23 mg
MCQs IN BIOCHEMISTRY
151.In human
(A)Liver
(B)Kidney
(C)Inte
stine(D)
152.In human
(A)NAD
(B)FAD
(C)Pyridoxal phosphate
(D)Biotin
(A)Thyroid gland as thyroglobulin
(B)Liver
(C)Intestine
(D)Skin
(A)T
(B)PTH
(C)Insulin
(D)Adrenaline
(A)5-vinyl-2 thio oxalzolidone
(B)Pyridine-3-carboxylic acid
MCQs IN BIOCHEMISTRY
(A)Respiratory alkalosis
(B)Respiratory acidosis
MCQs IN BIOCHEMISTRY
MCQs IN BIOCHEMISTRY
258.T
(A)Hyperparathyroidism
(B)Intestinal malabsorption
(C)Osteomalacia
(D)Chronic renal failure
MCQs IN BIOCHEMISTRY
(A)Four subunits(B)Eight subunits
(C)Ten subunits
(D)Twenty-four subunits
(A)Intestinal mucosa(B)
(C)Spleen
(D)All of these
(A)Ferritin and transferrin
(B)Transferrin and haemosiderin
(C)Haemoglobin and myoglobin
(D)Ferritin and haemosiderin
(A)Ferritin
(B)Haemosiderin
(C)Transfer
rin(D)Haemoglobin
(A)40,000(B)60,000
(C)80,000(D)1,00,000
(A)50100
g/dl(B)100150
(C)50175
g/dl(D)250400
(A)Peroxidase(B)
(C)Aconitase(D)
299.T
(A)0.1 mg(B)1 mg
(C)5 mg
(D)10 mg
(A)Ascorbic acid(B)Succinic acid
(C)Phytic acid(D)Amino acid
(A)In achlorhydria
(B)When ferritin content of intestinal mucosa is
(C)When saturation of plasma transferring is low
(A)1–3 mg(B)4–8 mg
(C)10–15 mg(D)25–30 mg
(A)50
(B)100
(C)150
g(D)1 mg
(A)Patients with hyperthyroidism
(B)Patients with hypothyroidism
(C)Pregnant women
(D)Goitre belt areas
(A)It occurs in areas where soil and water have
(B)It leads to enlargement of thyroid gland
(C)It results ultimately in hyperthyroidism
(D)It can be prevented by consumption of
(A)1 gm
(B)500 mg
(C)100 mg(D)10 mg
(A)25–50
g/dl(B)50–100
(C)100–200
g/dl(D)200–400
(A)Polycythaemia(B)Leukocytopenia
(C)Thrombocytopenia(D)
(A)0.5 mg(B)1 mg
(C)2.5 mg(D)5 mg
(A)It is a copper-containing protein
(B)It possesses oxidase activity
(C)It is synthesised in intestinal mucosa
(D)Its plasma level is decreased inWilson’s
Wilson’s disease are correct except
MCQs IN BIOCHEMISTRY
(A)Copper(B)
(C)Zinc(D)
(A)Selenium(B)Copper
(C)Zinc
(D)Cobalt
(A)Zinc
(B)Copper
(C)Manganese(D)
(A)1–2 mg(B)2–5 mg
(C)2–5 µg(D)5–20 µg
(A)Xanthine oxidase(B)Aldehyde oxidase
(C)Sulphite oxidase(D)All of these
334.A
(A)Selenium(B)
Tocopherol
(C)Chromium(D)
(A)Glutathione reductase
(B)Glutathione peroxidase
(C)Catalase
(D)Superoxide dismutase
(A)Copper(B)Zinc
(C)Vitamin D(D)Vitamin E
(A)0.4 ppm(B)0.8 ppm
(C)1.2 ppm(D)2 ppm
(A)0.5 mg(B)1 mg
(C)2 mg
(D)3 mg
339.In
(A)50% of body weight
(B)55% of body weight
(C)60% of body weight
(D)75% of body weight
340.1
(A)4.2 J
(B)42 J
(C)4.2 KJ
(D)42 KJ
349.At a
(A)5.825 kcal(B)4.825 kcal
(C)3.825 kcal(D)2.825 kcal
MCQs IN BIOCHEMISTRY
369.A
(A)40 mg
(B)440 mg
(C)160 mg(D)365 mg
370.T
(A)1-2 gm
(B)3-4 gm
(C)4-5 gm(D)7-10 gm
385.In
case of wilson’s disease, the features
(A)Progressive hepatic cirrhosis
(B)Keyser Fleisher ring
(C)Aminoaciduria
MCQs IN BIOCHEMISTRY
402.What
in the serum?
(A)137–148 mEq/L(B)120–160 mEq/L
(C)3.9–5.0 mEq/L(D)0.3–0.59 mEq/L
(A)The structural components of body tissues
(B)In the regulation of body fluids
(C)In acid-base balance
(D)All of these
(A)In muscle contraction
(B)Cell membrane function
(C)Enzyme action
(D)All of these
(A)200 mg(B)400 mg
(C)800 mg(D)600 mg
406.The
(A)1.5–2.5 mg/100 ml
(B)2.5–4.5 mg/100 ml
(C)4.5–6.5 mg/100 ml
(D)0.5–1.5 mg/100 ml
(A)In hyper thyroidism(B)Cirrosis of liver
(C)Leukemia(D)
(A)Coenzyme
(B)One of the component of photophosphorylation
(C)It is the stored form of iron
1. A
4. A
8. B
10. D
15. B
18. D
19. D
32. A
34. A
35. B
43. D
45. B
48. D
49. D
51. D
55. D
56. B
57. B
60. D
61. A
64. D
65. B
66. D
69. C
70. D
71. A
72. B
73. C
76. B
77. A
78. C
80. D
85. C
87. A
88. C
89. D
90. D
93. D
99. D100. A
101. C102. A
103. B104. B
C108. B
109. A110. D
111. C112. D
113. A114. B
115. A116. A
117. D118. A
119. D120. D
121. B122. A
123. A124. B
125. A126. A
127. A128. C
129. A130. A
131. B132. C
133. D134. C
135. C136. C
137. A138. B
139. A140. B
C144. C
145. D146. D
147. B
C150. D
151. C152. C
155. A156. C
157. D158. B
159. A
C162. D
163. A164. C
165. C166. A
167. A168. D
169. A170. D
171. A172. A
173. A174. A
175. B176. A
177. A178. C
179. A180. C
181. D182. B
183. A184. D
185. C186. A
187. B188. C
C192. D
193. A194. D
195. D196. D
197. A198. A
199. A200. C
201. B202. A
203. D204. A
205. A206. B
B210. C
211. A212. C
213. B214. A
215. B216. A
217. A218. A
219. B220. D
221. A222. A
223. B224. D
227. C228. A
229. C230. A
C234. D
235. A236. C
237. A238. B
239. A240. B
241. D242. B
243. A244. A
245. A246. A
247. C248. A
249. A250. D
251. D252. B
MCQs IN BIOCHEMISTRY
253. D254. C
255. D256. C
257. C258. D
259. A260. B
261. D
263. C264. C
265. D266. C
267. D268. D
269. A270. C
271. A272. D
275. C276. D
277. D278. D
279. C280. A
281. D282. A
283. B284. B
285. C286. C
287. C288. C
289. B290. C
293. D294. D
295. C296. C
B300. C
301. A302. C
303. D304. A
305. D306. B
307. B308. D
311. C312. C
313. D314. C
315. C316. C
317. D318. C
319. C320. D
321. C322. C
323. B324. B
325. D326. D
327. C328. D
329. C330. C
331. B332. B
333. D334. A
335. B336. D
337. C338. D
339. C340. C
341. C342. D
343. C344. D
345. D346. B
347. C348. D
349. B350. C
353. B354. D
355. A356. C
359. D360. A
361. C362. D
363. B364. B
365. C366. D
367. A368. C
B372. D
373. C374. C
375. C376. A
377. C378. B
379. D380. B
381. B382. C
383. D384. B
385. D386. A
389. C390. B
391. D392. B
D396. D
397. B398. D
401. A402. C
403. D404. D
405. C406. B
407. A408. C
409. C410. D
411. D412. A
413. B414. C
1.Hormones
(A)Act as coenzyme
(B)Act as enzyme
(C)Influence synthesis of enzymes
(D)Belong to B-complex group
2.Hormone that binds to intracellular
(A)Adrenocorticotropic hormone
(B)Thyroxine
(C)Follicle stimulating hormone
(D)Glucagon
3.Hormone that bind to cell surface receptor
CHAPTER 8
CHAPTER 8
CHAPTER 8
CHAPTER 8
HH
HH
ORMONEORMONE
ORMONEORMONE


MM
MM
MCQs IN BIOCHEMISTRY
12.Biological activity of ACTH requires
(A)10-N-terminal amino acid
(B)24-N-terminal amino acid
(C)24-C-terminal amino acid
(D)15-C-terminal amino acid
28.3-
ββ
ββ
∆∆
∆∆
(A)Androstenedione(B)
Testosterone
(C)Progesterone
(D)Estrone
29.In the resting state plasma concentration
(A)0.4–2.0
(B)2.0–4.0
(C)5.0–15.0
(D)18.0–25.0
30.The most important effect of aldosterone
(A)Increase the rate of tubular reabsorption of
(B)Decrease the rate of tubular reabsorption of
(C)Decrease the reabsorption of chloride
(D)Decrease the renal reabsorption of sodium
31.One of the potent stimulators of
MCQs IN BIOCHEMISTRY
44.Increased reabsorption of water from the
60.The normal serum level of thyroxine (T
(A)2.0–4.0
(B)5.5–13.5
(C)14.0–20.3
(D)20.0–25.0
MCQs IN BIOCHEMISTRY
78.The characteristic of hyperparathyroidism
(A)Low serum calcium
(B)High serum phosphorous
(C)Low serum calcium and high serum phos-
(D)High serum calcium and low serum
79.Parathyroid hormone
(A)Is released when serum Ca
(B)Inactivates vitamin D
96.Insulin stimulates
(A)Hepatic glycogenolysis
(B)Hepatic glycogenesis
(C)Lipolysis
(D)Gluconeogenesis
MCQs IN BIOCHEMISTRY
Normal serum free testosterone in adult
130.The p
(A)Aldosterone(B)
MCQs IN BIOCHEMISTRY
(A)Nerve growth factor
162.A
(A)Melatonin
(B)Melanocyte stimulating hormone
(C)Vasopressin
(D)Prolactin
MCQs IN BIOCHEMISTRY
179.All the following statements about ACTH
(A)It is a tropic hormone
(A)Overgrowth of the bones of face, hands and
MCQs IN BIOCHEMISTRY
(A)Goitre, heat intolerance, weight loss and
(B)Goitre, tremors, tachycardia and cold
(C)Exophthalmos, goiter, tachycardia and loss
αα
αα
(A)Outside the cell membrane
(B)In the cell membrane
(C)Across the cell membrane
(D)In the cytosol
ββ
ββ
(A)Outside the cell membrane
(B)In the cell membrane
(C)Across the cell membrane
(D)In the cytosol
228.In
the insulin receptor, tyrosine kinase
-Subunits(B)
-Subunits(D)
(A)Adenylate cyclase(B)Guanylate cyclase
(C)Phospholipase C(D)Tyr
(A)One
(B)Two
(C)Two,
α
(D)One
(A)Muscle cells(B)Renal tubular cells
(C)Adipocytes(D)
(A)Glycogenesis
(B)Glyolysis
(C)Gluconeogenesis
(D)Tubular reabsorption of glucose
(A)Glycogenesis
(B)Gluconeogenesis
(C)Lipolysis(D)
(A)Protein synthesis(B)
(C)Glycogen synthesis(D)
(A)Hexokinase
(B)Glucokinase
(C)PEP carboxykinase
MCQs IN BIOCHEMISTRY
(A)Dihydroxyphenylalanine
(B)Epinephrine
(C)Norepinephrine
(A)Glucocorticoid(B)Mineralocorticoid
(C)Androgen(D)
(A)Hydrocortisone(B)
(C)Aldactone A(D)
260.Steroid
(A)Testes
(C)Adrenal medulla
(D)Adrenal cortex
(A)Cholesterol
(B)7-Dehydrocholesterol
(C)Calcitriol
(D)7-Hydroxycholesterol
262.A
(A)Pregnenolone
(B)17-Hydroxypregnenolone
(C)Corticosterone
(D)Progesterone
263.A
(A)Progesterone(B)
Testosterone
(C)Estradiol(D)
264.A
(A)Cortisol
(B)Andostenedione
(C)Corticosterone
(D)11-Deoxycorticosterone
(A)In association with transcortin chiefly
(B)In association with albumin to some extent
(C)In free form partly
(D)All of these
(A)It is synthesised in liver
(B)It transports glucocorticoids
(C)It transports aldosterone
(D)It transports progesterone
(A)Cyclic AMP
(B)Cyclic GMP
(C)Inositol triphosphate
(D)No second messenger is required
(A)Gluconeogenesis
(B)Lipolysis in extremities
(C)Synthesis of elcosanoida
(D)Hepatic glycogenesis
(A)Glucokinase
(B)Glucose-6-phosphatase
(C)Fructose-1, 6-biphosphatase
(D)Pyruvate carboxylase
MCQs IN BIOCHEMISTRY
Mineralocorticoids increase the tubular
(A)Five amino acids
(B)Twelve amino acids
(C)Seventeen amino acids
(D)Twenty amino acids
(A)Four N-terminal amino acids
(B)Four C-terminal amino acids
(C)Five N-terminal amino acids
(D)Five C-terminal amino acids
ββ
ββ
(A)It is a polypeptide
(B)Its precursor is pro-opio-melanocortin
(C)Its receptors are represent in brain
(D)Its action is blocked by morphine
(A)It is a protein
(B)It possess quaternary structure
(C)Its receptor is made up of a single polypep-
(D)Its receptor possesses tyrosine kinase domain
MCQs IN BIOCHEMISTRY
307.STAT pr
(A)Thermostat proteins of brain
(B)Glucostat proteins of hepatocyte cell
(C)Short term activators of translation
(D)Signal transduction and activators of
(A)Phosphatidyl inositol-4, 5-biphosphate
(B)Inositol-1, 4, 5-triphosphate
(C)Protein kinase C
(D)Pl-3 kinase
(A)G
proteins(B)G
(C)G
proteins(D)G
(A)Glucosamine
(B)Mannosamine
(C)Sialic acid(D)M
(A)Cystic fibrosis(B)
(C)Acute pancreatitis(D)
(A)It is inherited as an autosomal recessive
(B)It affects a number of exocrine glands
(C)It causes increased sweating
(D)Sweat chlorides are above 60 mEq/L in this
(A)1.5–15% of the test done
(B)15–20% of the test done
(C)20–40% of the test done
(D)50–70% of the test done
(A)Endemic goitre(B)
(C)Myxoedema(D)
(A)0.8–2.4 ng/dl(B)0.8–2.4
(C)5–12 ng/dl(D)5–12
316.Normal range of
(A)0.1–0.2 ng/dl(B)0.1–0.2
(C)0.8–2.4 ng/dl(D)0.8–2.4
(A)Hyperthyroidism of pituitary origin
(B)Hyperthyroidism of thyroid origin
(C)Hypothyroidism of pituitary origin
(D)Hypothyroidism of thyroid origin
(A)Hyperthyroidism of pituitary origin
(B)Hypothyroidism of pituitary origin
(C)Hyperthyroidism of thyroid origin
(D)Hypothyroidism of thyroid origin
(A)Endemic goitre(B)
(C)Myxoedema(D)Cret
(A)If uses DNA polymerase with nuclease
(B)It is replicated bidirectionally at many points
The most potent hormone concerned with
MCQs IN BIOCHEMISTRY
339.Tyr
(A)Potassium Iodide
(B)Iodine
(C)Iodide I
(D)Higher valency state of iodine (I
(A)Epinephrine
(B)Glucagon
(C)Parathyroid hormone
(D)Insulin
(A)adrenal medulla
(B)bone
(C)head of Pancreas
(D)pituitary
Which one of
(A)Insulin increases glucose phosphorylation
(B)Insulin increases glycolysis
(C)Insulin augments HMP shunt
(D)Insulin promotes gluconeogenesis
(A)Androgens
(B)Estrogens
(C)Cholesterol(D)
(A)Motiline
(A)3–8 mg(B)4–8 mg
(C)3–8 gm(D)4–8 gm
(A)C
(B)C
(C)C
(D)C
(A)Voneuler
(B)Sultan Karim
MCQs IN BIOCHEMISTRY
(A)Pro-opiomelanocortin
(D)Endorphins
α, β α, β
α, β α, β
α, β
J J
J J
(A)Pro-opiomelanocortin
(C)ATCH
(D)Lipoprotein
(A)Serotonin(B)N
(C)Dopanine(D)
(A)Testosteron(B)
(C)Calcitonine(D)Vasopressin
392.W
cushing’s syndrome, a tumor associated
(A)Decreased production of epinephrine
(B)Excessive production of epinephrine
(C)Excessive production of vasopressin
(D)Excessive production of cortisol
393.A
(A)Interfere with synthesis of prostaglandins
(B)Decrease the effects of Glucagon
(C)Enhance the effects of epinephrine
(D)Provide the vitamin nicotinic acid
(A)Cortisol
(B)
(C)Vasopressin(D)Aldosterone
(A)Androstenadione deficiency
(B)Estrone deficiency
(C)17
(D)C-
(A)Cholera toxin
MCQs IN BIOCHEMISTRY
(A)Estrogens(B)Gluco corticoids
(C)MIS
(D)None of these
406.A
(A)Folic acid responsive
(B)Vitamin B
(C)Pyridoxine responsive
(D)Vitamin C responsive
1. C
2. B
6. C
7. A
10. D
56. D
62. B
63. D
68. B
69. A
71. C
74. B
78. D
82. D
90. D
91. C
92. B
93. D
95. A
96. B
99. A100. A
101. A102. B
103. D104. C
105. B106. B
107. A108. A
109. B110. C
111. C112. B
113. A114. C
115. C116. C
117. C118. B
119. C120. A
121. D122. C
123. B124. A
125. B126. A
127. A128. B
129. A130. D
131. B132. D
135. A136. A
137. D138. D
139. D140. A
141. D142. D
143. A144. B
145. C146. D
147. D148. C
149. C150. B
151. A152. B
153. D154. D
155. B156. C
157. C158. C
159. D160. B
161. C162. C
163. B164. A
165. C166. A
167. B168. C
169. A170. B
C174. D
175. C176. D
177. D178. C
179. D180. C
181. A182. B
183. D184. D
185. B186. B
187. A188. D
189. C190. A
191. B192. D
193. B194. B
195. C196. A
197. A198. C
199. B200. C
203. A204. C
205. D206. C
207. D208. D
209. A210. D
211. C212. A
213. A214. B
215. A216. B
217. A218. D
219. D220. C
221. D222. C
223. D224. A
225. A226. A
227. C228. B
229. D230. B
233. A234. D
235. C236. B
237. D238. A
239. A240. D
241. C242. A
D246. B
MCQs IN BIOCHEMISTRY
247. D248. C
249. A250. D
251. C252. A
253. A254. D
257. A258. B
259. C260. A
261. A262. A
263. A264. B
265. D266. C
267. D268. C
269. A270. C
271. C272. C
273. C274. B
275. B276. A
277. D278. C
279. A
281. B282. B
283. A284. B
285. A286. B
287. B288. C
289. D290. A
291. C292. B
293. D294. B
295. B296. C
297. B298. C
299. A300. A
301. A302. D
303. A304. B
305. B306. B
307. D308. A
309. C310. D
311. A312. C
313. C314. B
315. D316. B
317. C318. C
319. B320. C
323. B324. D
325. B326. D
327. B328. B
329. D330. A
331. B332. D
333. C334. A
335. B336. D
337. B338. C
339. D340. D
341. A342. D
343. B344. D
345. C346. B
347. A348. A
349. C350. D
351. B352. B
353. A354. A
355. A356. A
357. D358. B
359. A360. A
361. A362. D
365. D366. A
367. B368. C
C372. D
373. C374. A
375. B376. C
377. D378. D
379. C380. B
381. B382. B
383. D384. D
385. B386. A
D390. C
391. C392. D
393. C394. C
395. D396. A
397. B398. A
399. C400. B
401. A402. C
403. B404. C
B408. C
409. C410. D
411. B412. D
413. C
1.A nucleoside consists of
(A)Nitrogenous base
(B)Purine or pyrimidine base + sugar
(C)Purine or pyrimidine base + phosphorous
(D)Purine + pyrimidine base + sugar +
2.A nucleotide consists of
(A)A nitrogenous base like choline
(B)Purine + pyrimidine base + sugar +
(C)Purine or pyrimidine base + sugar
(D)Purine or pyrimidine base + phosphorous
3.A purine nucleotide is
(A)AMP
(B)UMP
(C)CMP
(D)TMP
4.A pyrimidine nucleotide is
(A)GMP
(B)AMP
(C)CMP
(D)IMP
5.Adenine is
(A)6-Amino purine
(B)2-Amino-6-oxypurine
(C)2-Oxy-4-aminopyrimidine
(D)2, 4-Dioxypyrimidine
6.2, 4-Dioxypyrimidine is
(A)Thymine
(B)Cystosine
(C)Uracil
(D)
CHAPTER 9
CHAPTER 9
CHAPTER 9
CHAPTER 9
NN
NN
UCLEICUCLEIC
UCLEICUCLEIC


AA
AA
CIDSCIDS
CIDSCIDS
7.The chemical name of guanine is
MCQs IN BIOCHEMISTRY
13.The mean intracellular concentration of
ATP in mammalian cell is about
(A)1 mM(B)2 mM
(C)0.1 mM(D)0.2 mM
14.The nucleic acid base found in mRNA but
(A)Adenine(B)
(C)Guanine(D)
15.In RNA moleule ‘Caps’
(A)Allow tRNA to be processed
(B)Are unique to eukaryotic mRNA
(C)Occur at the 3’ end of tRNA
(D)Allow correct translation of prokaryotic mRNA
16.In contrast to eukaryotic mRNA,
(A)Can be polycistronic
(B)Is synthesized with introns
(C)Can only be monocistronic
(D)Has a poly A tail
17.The size of small stable RNA ranges from
(A)0–40 nucleotides
(B)40–80 nucleotides
(C)90–300 nucleotides
(D)More than 320 nucleotides
18.The number of small stable RNAs per cell
(A)10–50,000
(B)50,000–1,00,000
(C)1,00,000–10,00,000
(D)More than 10 lakhs
31.Transfer RNAs are classified on the basis
(A)Acceptor arm(B)Anticodon arm
(C)D arm(D)Extra arm
32.In tRNA molecule D arm is named for the
(A)Uridine
(B)
(C)Dihydrouridine(D)Thymidine
33.The acceptor arm in the tRNA molecule has
(A)5 Base pairs(B)7 Base pairs
(C)10 Base pairs(D)20 Base pairs
34.In tRNA molecule, the anticodon arm
(A)5 Base pairs(B)7 Base pairs
(C)8 Base pairs(D)10 Base pairs
35.The T
(A)T, pseudouridine and C
(B)T, uridine and C
(C)T, dihydrouridine and C
(D)T, adenine and C
36.Double helical structure model of the DNA
(A)Pauling and Corey
MCQs IN BIOCHEMISTRY
64.Phosphorylation of adenosine to AMP is
(A)Adenosine kinase
(B)Deoxycytidine kinase
(C)Adenylosuccinase
MCQs IN BIOCHEMISTRY
79.Conversion of deoxyuridine monophos-
(A)Ribonucleotide reductase
94.Lesch-Nyhan syndrome, the sex linked,
recessive absence of HGPRTase, may lead
(A)Compulsive self destructive behaviour with
(B)Hypouricemia due to liver damage
(C)Failure to thrive and megaloblastic anemia
(D)Protein intolerance and hepatic encephalop-
95.The major catabolic product of pyrim-
-Alanine(B)Urea
(C)Uric acid
(D)Guanine
96.Orotic aciduria type I reflects the deficien-
(A)Orotate phosphoribosyl transferase and
(B)Dihydroorotate dehydrogenase
(C)Dihydroorotase
MCQs IN BIOCHEMISTRY
(A)Rho (
) factor(B)
factor(D)
110.In
(A)Initiation requires rho protein
122.Initiation of protein synthesis requires
(A)ATP
(B)AMP
(C)GDP
(D)GTP
MCQs IN BIOCHEMISTRY
135Streptomycin prevents synthesis of poly-
(A)Inhibiting initiation process
(B)Releasing premature polypeptide
(C)Inhibiting peptidyl transferase activity
(D)Inhibiting translocation
(A)Formation of initiation complex
(B)Binding of aminoacyl tRNA
(C)Peptidyl transferase activity
(D)Translocation
(A)Puromycin
(B)Rifamycin
(C)Terramycin(D)Streptomycin
(A)Structural(B)Regulator
(C)Promoter(D)Operator
139The gene of lac operon which has constitu-
(A)i
(B)c
(C)z
(D)p
140.The
(A)5 base pairs(B)10 base pairs
(C)15 base pairs(D)17 base pairs
141To commence structural gene transcrip-
(A)Promoter site(B)Operator locus
(C)Y gene(D)A gene
142.In
(A)Operator
(B)Inducer
(C)Promoter
(D)Repressor
(A)AMP
(B)GMP
(C)cAMP
(D)Cgmp
(A)Introduces superhelical twists
(B)Connects the end of two DNA chains
(C)Unwinds the double helix
(D)Synthesises RNA primers
(A)Cut RNA chains at specific locations
(B)Excise introns from hnRNA
(C)Remove Okazaki fragments
(D)Act as defensive enzymes to protect the host
(A)Is virus specific
(B)Is a bacterial product
MCQs IN BIOCHEMISTRY
(A)Z-DNA
(B)
(C)B-DNA
(D)
(A)Histones
(B)Non-histones
(C)Both (A) and (B)(D)None of these
(A)mRNA
(B)tRNA
(C)DNA
(D)None of these
(A)mRNA
(B)tRNA
(C)rRNA
(D)DNA
(A)Template strand of DNA
(B)mRNA
(C)tRNA
(D)rRNA
(A)5’-End
(B)3’-End
(C)Anticodon(D)
173.In
(A)30 S and 40 S(B)40 S and 50 S
(C)30 S and 50 S(D)40 S and 60 S
(A)Enzymes present in ribosomes
(B)Enzymes which combine the ribosomal
(C)Enzymes which dissociate
(D)Enzymes made up of RNA
(A)rRNA
(B)
(C)mRNA
(D)tRNA
176.The number of adenine and thymine bases
(A)DNA
(B)mRNA
(C)tRNA
(D)rRNA
187.De novo synthesis of purine nucleotide
(A)Mitochondria(B)
(C)Microsmes(D)Ribosomes
(A)Aspartate and glutamate
(B)Aspartate and glycine
(C)Aspartate, glutamine and glycine
(D)Aspartate, glutamate and glycine
189For de novo synthesis of purine nucle-
(A)One nitrogen atom
(B)One nitrogen and one carbon atom
(C)Two carbon atoms
(D)One nitrogen and two carbon atoms
(A)Nitrogen 1(B)Nitrogen 3
(C)Nitrogen 7(D)Nitrogen 9
191.In
(A)Glycine(B)CO
(C)Aspartate(D)Glutamine
(A)Purine nucleotides(B)
(C)Both (A) and (B)(D)None of these
(A)AMP and GMP(B)CMP and UMP
(C)CMP and TMP(D)All of these
(A)TMP
(B)CMP
(C)AMP
(D)GMP
195.In
(A)PRPP glutamyl amido transferase
MCQs IN BIOCHEMISTRY
(A)Adenine and guanine
(B)Adenine and hypoxanthine
(C)Guanine and hypoxanthine
(D)Adenine, guanine and hypoxanthine
(A)Adenine phosphoribosyl transferase
(B)Hypoxanthine guanine phosphoribosyl
(C)Both (A) and (B)
(D)None of these
(A)Adenosine
(B)Adenosine and deoxyadenosine
(C)Adenosine and guanosine
(D)Adenine and adenosine
(A)Adenosine
(B)Adenosine and deoxyadenosine
(C)Adenosine and guanosine
(D)Adenine and adenosine
(A)Adenosine phosphoribosyl transferase
(B)Hypoxanthine guanine phosphoribosyl
(C)Availability of PRPP
(D)None of these
209.The available PRPP is used preferentially
(A)De novo synthesis of purine nucleotides
(B)De novo synthesis of pyrimidine nucleotides
(C)Salvage of purine bases
(D)Salvage of pyrimidine bases
(A)Inosine
(B)Hypoxanthine
(C)Xanthine(D)Uric acid
211.The enzyme common to catabolism of all
(A)Adenosine deaminase
(B)Purine nucleoside phosphorylase
(C)Guanase
(D)None of these
(A)Man
(B)Fish
(C)Birds
(D)None of these
213.D
(A)Glutamine
(B)Glutamate
(C)Glycine(D)
(A)Glutamine
(B)Glutamate
(C)Glycine(D)
(A)CO
(B)Glycine
(C)Aspartate(D)Glutamine
(A)C
(B)C
(C)C
(D)C
(A)UMP
(B)CMP
(C)CTP
(D)TMP
(A)Ribonucleotide reductase
(B)Thioredoxin
MCQs IN BIOCHEMISTRY
235.Cytosolic carbamoyl phosphate syn-
(A)Oral administration of orotic acid
MCQs IN BIOCHEMISTRY
(A)Both the new strands are synthesized disconti-
(B)One strand is synthesized continuously and
(C)Both the new strands are synthesized
(D)RNA primer is required only for the synthesis
268.An
(A)10 Nucleotides
(B)100 Nucleotides
(C)1,000 Nucleotides
(D)10,000 Nucleotides
(A)Ribonuclease
(B)Primase
(C)DNA polymerase I(D)
270.In
(A)Cytosine(B)
(C)Thymine(D)Uracil
(A)At one of the ends(B)At both the ends
(C)At multiple sites(D)
(A)DNAA protein(B)DnaB protein
(C)DNAC
protein(D)
(A)Energy is provided by ATP
(B)Energy is provided by GTP
(C)Energy can be provided by either ATP or GTP
(D)No energy is required
(A)Rewinding of DNA and require ATP as a
(B)Rewinding of DNA but do not require any
(C)Unwinding of DNA and require ATP as a
(D)Unwinding of DNA but do not require any
(A)Single strand binding protein
(B)Double strand binding protein
(C)Rep protein
(D)DNAA protein
(A)DNA polymerase I
(B)DNA polymerase II
(C)DNA polymerase III holoenzyme
(D)All of these
(A)DNA polymerase I
(B)DNA polymerase II
(C)DNA polymerase III holoenzyme
(D)All of these
(A)DNA polymerase II
(B)DNA ligase
(C)DNA gyrase
(D)DNA topoisomerase II
279.Negative supercoils are introduced in DNA
(A)Helicase
(B)DNA ligase
(C)DNA gyrase
(D)DNA polymerase III holoenzyme
(A)DNA polymerase
(B)DNA polymerase
(C)Telomerase
(D)DNA polymerase II
DNA polymerase III holoenzyme possesses
(A)Polymerase activity
(B)3’
(C)5’
(D)3’
(A) Polymerase activity
(B)3’
(C)5’
(D)All of these
283.3’
oo
oo
5’ Exonuclease activity of DNA
(A)Removes ribonucleotides
(B)Adds deoxyribonucleotides
(C)Corrects errors in replication
(D)Hydrolyses DNA into mononucleotides
(A)It synthesizes DNA using RNA as a template
(B)It is also known as reverse transcriptase
(C)It synthesizes DNA in 5’
(D)It is present in all the viruses
(A)Synthesis of RNA
(B)Breakdown of RNA
(C)Synthesis of DNA
(D)Breakdown of DNA
286.DNA A
(A)Positively supercoiled DNA
(B)Negatively supercoiled DNA
(C)Both (A) and (B)
(D)None of these
(A)Relaxation of negatively supercoiled DNA
(B)Relaxation of positively supercoiled DNA
(C)Conversion of negatively supercoiled DNA
(D)Conversion of double helix into supercoiled
288.In
(A)S phase(B)G
(C)Mitotic Phase(D)G
289.Me
(A)Solid DNA becomes liquid
(B)Liquid DNA evaporates
(C)DNA changes from double helix into
(D)Native double helical DNA is denatured
(A)A and T content(B)G and C content
(C)Sugar content(D)Phosphate content
(A)A and T content(B)G and C content
(C)Sugar content(D)None of these
292.R
MCQs IN BIOCHEMISTRY
298.DNA-dependent RNA polymerase requires
the following for its catalytic activity:
(A)Mg
(B)Mn
(C)Both (A) and (B)(D)None of these
(C)Sigma factor
(D)Rho factor
α−
(C)Sigma factor
(D)Rho factor
(A)mRNA
(B)rRNA
(C)tRNA
(D)hnRNA
302.Mammalian RNA polymerase III synthesises
(A)rRNA
(B)mRNA
(C)tRNA
(D)hnRNA
303.In
(A)RNA polymerase I(B)RNA polymerase II
(C)RNA polymerase III(D)
(A)DNA polymerase
(B)DNA polymerase
(C)DNA polymerase
(D)DNA polymerase
(A)DNA
(B)mRNA
(C)tRNA
(D)rRNA
317.Ci
(A)DNA
(B)mRNA
(C)tRNA
(D)rRNA
(A)DNA topisomerase II
(B)DNA polymerase I
(C)DNA polymerase III
(D)DNA gyrase
(A)Unwinding of DNA
(B)Initiation of replication
(C)Initiation of translation
(D)Initiation of transcription
(A)Double stranded DNA
(B)Single stranded DNA
(C)Single stranded RNA
(D)DNA-RNA hybrid
321.DNA contains some palindromic sequences
(A)Mark the site for the formation of replication
(B)Direct DNA polymerase to turn back to
(C)Are recognized by restriction enzymes
(D)Are found only in bacterial DNA
(A)Encode the amino acids which are removed
(B)Encode signal sequences which are removed
MCQs IN BIOCHEMISTRY
(A)Upstream promoters
(B)Downstream promoters
(C)Intragenic promoters
(D)No promoters
(A)It is synthesized as a large precursor
(B)It is processed in the nucelolus
(C)It has no codons or anticodons
(D)Genes for rRNA are present in single copies
(A)Coding strand of DNA
(B)mRNA
(C)tRNA
(D)rRNA
(A)Non-coding strand of DNA
(B)hnRNA
(C)tRNA
(D)None of these
(A)mRNA
(B)tRNA
(C)rRNA
(D)
(B)Eukaryotic promoters
(C)Both (A) and (B)
(D)None of these
346.CAAT
(A)Prokaryotic promoters 10 bp upstream of
(B)Prokaryotic promoters 35 bp upstream of
(C)Eukaryotic promoters 25 bp upstream of
(D)Eukaryotic promoters 70–80 bp upstream of
(A)TATA box 25bp upstream of transcription start
(B)CAAT box 70-80 bp upstream of transcription
(C)Both (A) and (B)
(D)None of these
(A)A given tRNA can be charged with only one
(B)The amino acid is recognized by the
(C)The amino acid is attached to end of tRNA
(D)The anticodon of tRNA finds the comple-
mentary codon on mRNA
MCQs IN BIOCHEMISTRY
(A)ATPase activity(B)GTPase activity
(C)Helicase activity(D)
(A)Binds to 3’ chain initiation codon on mRNA
(B)Binds to 3’ end of mRNA
(C)Binds to 5’ end of mRNA
(D)Unwinds mRNA near its 5’ end
(A)40 S ribosomal subunit
(B)60 S ribosomal subunit
(C)eEF-2
(D)Amino acyl tRNA
(A)eEF-1 and GTP
(B)eEF-2 and GTP
(C)Peptidyl transferase and GTP
(D)Peptidyl transferase and ATP
(A)Streptomycin
(B)Chloramphenicol
(C)Erythromycin(D)Mitomycin
363.T
(C)Cis-acting elements
(D)Regulatory proteins
(A)Steroid hormones
(B)Calcitriol
(C)Histones
(D)Silencers
(A)Are trans-acting factors
MCQs IN BIOCHEMISTRY
388.La
(A)Attaching to i gene and preventing its
(B)Increasing the synthesis of catabolite gene
(C)Attaching to promoter region and facilitating
(D)Binding to repressor subunits so that the
(A)Lactose or its analogues
404.Amino acid sequence of the encoded
(A)Silent mutation
(B)Acceptable mis-sense mutation
(C)Both (A) and (B)
(D)None of these
(A)Silent mutation
(B)Acceptable mis-sense mutation
(C)Unacceptable mis-sense mutation
(D)Partially acceptable mis-sense mutation
406.If
(A)Silent mutation
(B)Acceptable mis-sense mutation
(C)Nonsense mutation
(D)Frameshift mutation
(A)Change in reading frame
(B)Garbled amino acid sequence in the
(C)Premature termination of translation
(D)All of these
408.A
MCQs IN BIOCHEMISTRY
(A)They are present in bacteria
(B)They act on double stranded DNA
(C)They recognize palindromic sequences
(D)They always produce sticky ends
5ATGCAG3
3TACGTC5
5CGAAGC3
3GCTTCG5
421.In
(A)The 2 strands of DNA are joined to each other
(B)The DNA strands stick to the restriction
(C)The ends of a double stranded fragment are
(D)The ends of a double stranded fragment are
(A)Plasmid
(B)Bacteriophage
(C)Baculovirus(D)
423.A
(A)Single stranded linear DNA
(B)Single stranded circular DNA
(C)Double stranded linear DNA
(D)Double stranded circular DNA
424.Fragments of DNA can be identified by the
(A)Western blotting(B)Eastern blotting
(C)Northern blotting(D)Southern blotting
425.A
(A)Western blotting(B)Eastern blotting
(C)Northern blotting(D)Southern blotting
426.A
(A)Southern blotting(B)Northern blotting
(C)Both (A) and (B)(D)None of these
427.An
(A)Southern blotting(B)Northern blotting
(C)Western blotting
(D)None of these
428.A
435.T
(B)Yeast
T.aquaticus
(D)Eukaryotes
444.B
(A)DNA B protein and ATP
(B)Helicase and ATP
(C)DNA topoisomerase I
(D)Alkali
T. aquaticus
(A)30°C
(B)37°C
(C)54°C
(D)72°C
447.In
addition to Taq polymerase, poly-
(A)A template DNA
(B)Deoxyribonucleoside triphosphates
(C)Primers
(D)Primase
DNA polymerase of T.aquaticus is
(A)It replicates DNA more efficiently
(B)It doesn’t require primers
(C)It is not denatured at the melting temperature
(D)It doesn’t cause errors in replication
449.T
(A)2
fold(B)20
(C)20 x 2 fold(D)20 fold
450.T
(A)Somatic cells of young animals
(B)Testes and ovaries of animals
(C)A viral vector and infecting the animals with
(D)Fertilised egg and implanting the egg into a
MCQs IN BIOCHEMISTRY
451.Y
east artificial chromosome can be used
(A)Upto 10 kb(B)Upto 45 kb
(C)Upto 100 kb(D)Upto 1,000 kb
(A)Constant number of tandem repeats
(B)Varibale number of tandem repeats
(C)Non-repititive sequences in each DNA
(D)Introns in eukaryotic DNA
(A)It results from mutations in restriction sites
(B)Mutations in restriction sites can occur in
(C)It is inherited in Mendelian fashion
Glycoproteins are marked for destruction
by removal of their
MCQs IN BIOCHEMISTRY
(C)Children who have inherited one mutation
497.The antibiotic which has a structure similar
(A)Actinomycin d
(B)Streptomycin
(C)Puromycin(D)Mitomycin c
498.ATP is r
(A)Fusion of 40S and 60S of ribosome
(B)Accommodation tRNA amino acid in a site of
(C)Movement of ribosome along mRNA
(D)formation of tRNA amino acid complex
(A)Chromosomes(B)Lymosomes
(C)Ribosomes(D)Centrosomes
500.An animal is in
(A)Intake exceeds output
(B)New tissue is being synthesized
(C)Output exceeds intake
(D)Intake is equal to output
is perfused through a dog’s
formed in the birds liver.
(A)Urea, Uric acid(B)Urea, allantoin
(C)Uric acid, creatinine
(D)Uric acid, Urea
(A)Glutamic acid and pyruvic acid
MCQs IN BIOCHEMISTRY
528.In
(A)Mitochondrian
MCQs IN BIOCHEMISTRY
(A)Cyclic AMP
(B)ATP
(C)DNA
(D)Inosine monophosphate
547.If
(A)Alpha
(B)
(A)Plant nucei
(B)Cardiac muscle cytoplasm
MCQs IN BIOCHEMISTRY
580.A
by inhibiting the enzyme Xanthine oxi-
dase is
(A)Aspirin
(B)
(C)Colchicine(D)
(A)C
(B)C
(C)C
(D)C
(A)Cytosine and Uric acid
(B)Adenylve acid and Glucine floc acid
(C)Orotic acid and Uridylic acid
(D)Adenosine acid Thymidine
(A)Glutamine and Carbamoyl-p
(B)Asparate and Carbamoyl-p
(C)Glutamate and NH
(D)Glutamine and NH
(A)Produces self-mutilation
(A)Amino acid activation
(B)Initiation of protein synthesis
(C)Termination of protein synthesis
(D)Elongation of polypeptide chains
(A)The ‘a’ gene(B)The ‘i’ gene
(C)The ‘c’ gene(D)The ‘z’ gene
597.In
MCQs IN BIOCHEMISTRY
(A)Glycoprotein synthesis
(B)ATP synthesis
(C)DNA synthesis
(D)mRNA synthesis
(A)One
(B)Two
(C)Three
(D)
613.T
(A)mRNA
(B)tRNA
(C)rRNA
(D)A
(A)mRNA
(B)GTP
3. A
5. A
8. D
10. D
14. D
15. B
21. B
24. D
31. D
33. B
40. D
45. D
51. D
54. D
55. D
57. D
60. D
69. B
78. D
86. D
92. B
99. D100. A
101. B102. A
103. B104. B
105. A106. B
107. C108. A
109. D110. C
111. D112. A
113. B114. A
115. B116. A
117. D118. A
119. A120. C
121. A122. D
123. B124. C
125. A126. A
127. D128. C
129. A
131. B132. B
133. D134. A
135. A136. D
137. B138. B
139. A140. D
141. B142. D
143. C144. B
145. D146. B
147. B148. B
149. D150. D
151. D152. A
153. C
155. B156. C
157. B158. A
159. A160. A
161. C162. C
163. C164. C
165. D166. C
167. A168. C
169. C170. D
171. B172. B
173. C174. D
175. D176. A
177. B
D180. C
181. B182. B
185. A186. D
187. B188. C
189. D190. A
191. B192. C
193. A194. D
197. D198. C
199. A200. C
201. D202. C
203. B204. D
205. C206. D
207. B208. C
209. C210. D
211. B212. C
213. D214. C
215. B216. B
217. D218. B
219. D220. A
221. A222. D
223. A224. C
225. A226. B
227. C228. C
229. D230. B
231. C232. A
233. C234. A
235. B236. A
237. C238. C
239. D240. D
241. B242. C
243. D244. C
245. C246. B
247. A248. C
249. A250. D
251. A252. C
MCQs IN BIOCHEMISTRY
253. D254. D
255. C256. C
257. C258. D
259. D260. A
261. B262. B
263. A264. A
265. C266. D
267. B268. C
269. B270. D
271. C272. B
273. A274. C
275. A276. C
277. A278. B
279. C280. C
281. D282. D
283. C284. D
285. C286. B
287. A288. A
289. D290. B
293. B294. A
295. C296. A
297. D298. C
299. C300. D
301. B302. C
305. C306. D
307. D308. B
311. A312. C
313. A314. B
315. B316. A
317. A318. D
319. D320. A
321. C
323. C324. C
325. A326. D
327. A328. B
329. C330. D
331. C332. B
333. A334. D
335. D336. C
337. A338. C
C342. D
343. A344. A
C348. B
349. B350. D
351. A352. B
353. D354. C
355. A356. B
357. D358. A
359. D360. B
361. B362. A
363. A364. C
365. C366. C
367. D368. D
369. B370. B
371. B372. C
373. B374. D
375. C376. B
377. B378. D
379. D380. B
D384. C
385. B386. B
C390. D
391. C392. D
393. A394. C
395. D396. A
397. B398. B
401. D402. B
403. D404. A
405. D406. C
407. D408. C
409. D410. A
411. C
413. A414. C
415. D416. B
417. C418. A
419. D420. C
421. C422. D
423. D424. D
425. C426. C
427. C428. C
429. D430. C
431. B432. C
433. D434. C
435. C436. B
437. D438. C
439. B440. C
441. C442. A
443. C444. C
445. D446. D
449. A450. D
451. D452. B
453. D454. D
455. B456. C
457. A458. D
459. B460. A
461. C462. D
463. C464. B
B468. D
469. A470. A
471. B472. D
473. D474. C
475. C476. D
479. C480. C
481. D482. D
483. C484. C
485. B486. D
487. A488. B
489. D490. A
491. B492. B
493. A494. D
C498. D
499. C500. C
501. A502. B
503. D504. D
505. C506. C
507. A508. C
509. C510. B
511. B512. A
513. D514. B
515. D516. B
517. D518. C
519. B520. B
521. B522. C
523. C524. B
525. C526. C
527. C528. A
529. C530. B
531. D532. A
533. A534. B
535. C536. C
538. B
539. D540. D
541. B542. B
545. A546. C
547. A548. B
C552. D
553. C554. A
555. D
557. C558. A
559. B560. C
561. C562. A
563. A564. A
565. A566. C
D570. B
571. B572. A
C576. D
577. A578. A
579. D
581. C582. B
583. C584. D
585. B586. D
587. A588. B
589. B590. B
591. D592. B
593. B594. D
595. C596. B
597. D598. B
599. A600. C
601. B602. B
603. D
605. B606. C
607. B608. D
609. B610. A
611. D612. B
613. D614. C
615. C616. B
617. A618. A
619. A620. D
intentionally left
blank
1.The total body water in various subjects
(A).30%
(B)40%
(C)50%
(D)70%
2..The percentage of water contained in the
(A)High fat content(B)Low fat content
(C)High protein content(D)
3.In intracellular compartment the fluid
(A)100
(B)200
(C)200
(D)330
4.In extra cellular compartment, the fluid
(A)120
(B)220
(C)270
(D)330
5.Fluid present in dense connective tissue
(A)10
(B)20
(C)45
(D)55
6.The total body water in ml/kg body
(A)200
(B)400
(C)600
(D)1000
CHAPTER 10
CHAPTER 10
CHAPTER 10
CHAPTER 10
WW
WW
AA
AA
TERTER
TERTER


&&
&&


EE
EE
LECTROLLECTROL
LECTROLLECTROL
YTEYTE
YTEYTE


BB
BB
ALANCEALANCE
ALANCEALANCE
7.The fluid present in bones which can not
(A)20 ml/kg(B)25 ml/kg
(C)45 ml/kg(D)60 ml/kg
MCQs IN BIOCHEMISTRY
13.The daily water allowance for normal
(A)200–600 ml(B)500–800 ml
(C)800–1500 ml(D)1800–2500 ml
14.Insensible loss of body water of normal
(A)50–100 ml(B)100–200 ml
(C)300–500 ml(D)600–1000 ml
15.The predominant cation of plasma is
(A)Na
(B)K
(C)Ca
(D)Mg
16.The predominant action of plasma is
(A)HCO
–(B)Cl–
(C)HPO
– –(D)SO
17.Vasopressin (ADH)
(A)Enhance facultative reabsorption of water
(B)Decreases reabsorption of water
WATER AND ELECTROLYTE BALANCE
30.The element needed in quantities greater
(A)Calcium(B)Zinc
(C)Selenium(D)Cobalt
31.The mineral present in the human body
(A)Sodium(B)Calcium
(C)Potassium(D)
32.The percentage of the total body calcium
(A)1
(B)11
(C)55
(D)99
33.The percentage of calcium present in
(A)1
(B)5
(C)10
(D)50
34.The physiologically active form of calcium
(A)Protein bond
(B)Ionised
(C)Complexed with citrate
(D)Complexed with carbonate
35.The normal concentration of calcium in
(A)1.5–2.5 mg/100 ml
(B)2.5–4 mg/100 ml
(C)4.5–5 mg/100 ml
(D)9–10 mg/100 ml
36.Absorption of calcium is increased on a
MCQs IN BIOCHEMISTRY
48.The normal concentration of magnesium
(A)1 mg/100 ml(B)3 mg/100 ml
(C)5 mg/100 ml(D)8 mg/100 ml
49.The magnesium content of muscle is about
(A)5 mg/100 ml(B)10 mg/100 ml
(C)21 mg/100 ml(D)50 mg/100 ml
50.Intestinal absorption of magnesium is
WATER AND ELECTROLYTE BALANCE
MCQs IN BIOCHEMISTRY
82.The percentage of CO
(A)20(B)40
(C)60(D)80
83.The normal serum CO
(A)18–20 meq/L(B)24–29 meq/L
(C)30–34 meq/L(D)35–38 meq/L
84.The carbondioxide carrying power of the
(A)50%
(B)60%
(C)85%
(D)100%
85.Within the red blood cells the buffering
(A)5%
(B)10%
(C)20%
(D)25%
WATER AND ELECTROLYTE BALANCE
MCQs IN BIOCHEMISTRY
Respiratory acidosis results from
WATER AND ELECTROLYTE BALANCE
During compensation of respiratory
alkalosis, all the following changes occur
MCQs IN BIOCHEMISTRY
1. D
2. A
3. D
8. D
9. B
13. D
14. D
19. D
21. B
24. D
26. B
32. D
42. D
44. B
45. D
55. D
60. D
64. C
65. A
66. A
69. B
72. D
74. B
76. D
85. D
86. D
91. D
99. B100. A
101. B102. D
103. D104. D
105. B106. D
107. B108. A
109. B110. C
111. B112. A
113. C114. C
115. A116. B
117. B118. C
119. B120. C
121. B122. A
123. B124. B
125. C126. A
127. D128. D
129. C130. D
131. D132. C
133. D134. D
135. A136. D
137. A138. D
139. B140. A

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