CHEMISTRY MCQs (PART 3)
CHEMISTRY MCQs (PART 3)
85. Optically active compounds are capable of
(A) Different reactions
(B) Rotating plane of polarized light
(C) Showing same chemical properties
(D) None of these
86. The reference compound for absolute configuration of
optically active compound is
(A) Alanine
(B) Lactic acid
(C) Glyceraldehyde
(D) Dihydroxy acetone
87. All the standard amino acids except the following have
one chiral ‘c’ atom:
(A) Threonine, Isoleucine
(B) Isoleucine, Alanine
(C) Threonine, Alanine
(D) Alanine, Glutamine
88. The role of complement proteins:
(A) Defense
(B) Helps immunity of the body
(C) Not predicatable
(D) None of these
89. Optical isomers that are mirror images and non
superimposable are called
(A) Diastereomers
(B) Euantiomers
(C) dl isomers
(D) Stereomers
90. Living cells have the unique ability to synthesize only
_________ the form of optical isomer due to _________.
(A) ‘d’ form, stereospecific enzymes
(B) ‘l’ form stereospecific enzymes
(C) ‘d’ form, DNA
(D) ‘L’ form, DNA
91. Isoelectric pH of an amino acid is that pH at which it
has a
(A) Positive charge
(B) Negative charge
(C) No net charge
(D) All of these
92. Albuminoids are similar to
(A) Albumin
(B) Globulin
(C) Both A and B
(D) None of these
93. Abnormal chain of amino acids in sickle cells anaemia is
(A) Alpha chain
(B) Beta chain
(C) Gama chain
(D) Delta chain
94. In prehepatic jaundice, protein flocculation test is
(A) Normal/weekly positive
(B) Usually positive
(C) Negative
(D) None of these
95. Side chains of all amino acids contain aromatic rings
except
(A) Pheynl alanine
(B) Alanine
(C) Tyrosine
(D) Tryptophan
96. In Nitroprusside test, amino acid cystein produces
(A) Blue colour
complex
(B) Red colour
(C) Yellow colour
(D) Purple colour
97. Bonds that are formed between two cysteine residues is
(A) Disulphide
(B) Peptide
(C) Electrostatic
(D) Hydrophobic
98. The acid amide of Aspartic acid is
(A) Glutamine
(B) Arginine
(C) Aspargine
(D) Ornithine
99. It is the only amino acid having an ionizing ‘R’ group
with a pK’ near 7 and is important in the active site of some enzymes:
(A) Arginine
(B) Cystein
(C) Cystine
(D) Histidine
100. Hemoglobin has a high content of this amino acid:
(A) Proline
(B) Leucine
(C) Arginine
(D) Histicline
101. A hexa peptide with 5 aspartic acid would have a net
charge at pH 7:
(A) Neutral
(B) Positive
(C) Negative
(D) Not predictable
102. In the genetic disorder of cystinuria, the patient
excretes large quantities of cystine in their urine and its low solubility
causes crystalline cystine to precipitate as stones in kidneys. The remedy
involves
ingesting Na HCO3. Reaction of this treatment is
(A) NaHCO2 combines with cystine
(B) NaHCO3 raises the pH above the isoelectric point of
cystine
(C) NaHCO3 prevents stone formation by hydrolysis of cystine
to cysteine
(D) None of these
103. In the following reaction, Alanine acts as a 3 3 3 3 +
+ → H H | | H N – – COO —— H N – – COOH C C | | CH CH
(A) Acid
(B) Base
(C) Zwitter ion
(D) None of these
104. Amino acids excepting histidine are not good buffering
agents in cell because
(A) They exist as zwitter ions
(B) Their pk and not
in the physiological pH of a cell
(C) Only Histidine has pk of its R group at 6.0 unlike the
others which have at a different pH
(D) None of these
105. At neutral pH Alanine has the following structure:
(A) − − 2 3 H H N C COOH CH
(B) + 3 − − 3 H H N C COO CH
(C) 2 − − 3 H H N C COO CH
(D) + 2 − − 3 H H N C COO CH
106. The amino acids in which the R groups have a net
positive charge at pH 7.0 are
(A) Lysine, Arginine, Histidine
(B) Lysine, Aspargine
(C) Histidine, Aspargine
(D) Glutamine, Arginine
107. Apolipoproteins are
(A) AI
(B) AI1
(C) C1
(D) All of these
108. The amino acid which has a pK near 4 and thus is
negatively charged at pH 7 is
(A) Alanine
(B) Glutamic acid
(C) Glutamine
(D) Aspargine
109. The side chain of which of the following amino acid
contain sulphur atom?
(A) Methionine
(B) Threonine
(C) Leucine
(D) Tryptophan
110. Which of the followings gives a positive test for
Ninhydrin?
(A) Reducing sugars
(B) Triglycerides
(C) Alpha aminoacids
(D) Esterified Fats
111. In glutathione (a tripeptide) is present apart from
Glutamic acid and cysteine:
(A) Serine
(B) Glycine
(C) Leucine
(D) Phenyl alanine
112. 2-Amino 3-OH propanoic acid is
(A) Glycine
(B) Alanine
(C) Valine
(D) Serine
113. All amino acids have one asymmetric carbon atom, except
(A) Arginine
(B) Aspargine
(C) Histidine
(D) Glycine
114. Number of amino acids present in the plant, animal and
microbial proteins:
(A) 20
(B) 80
(C) 150
(D) 200
115. Immunoglobulins are characterized by their
(A) Heavy chains
(B) Molecular weight
(C) Light chains
(D) Electrophoretic behavior
116. The bond in proteins that is not hydrolysed under usual
conditions of denaturation:
(A) Hydrophobic bond
(B) Hydrogen bond
(C) Disulphide bond
(D) Peptide bonds
117. If the amino group and a carboxylic group of the amino
acid are attached to same carbon atom, the amino acid is called
(A) Alpha
(B) Beta
(C) Gamma
(D) Delta
118. Zymogen is
(A) An intracellular enzyme
(B) Serum enzyme
(C) A complete extracellular enzyme
(D) An inactivated enzyme
119. SGOT level in a adult is
(A) 5–40 units/dl
(B) 1–4 units/dl
(C) 5–15 units/dl
(D) 50–100 units/dl
120. Activity of ceruloplasmin shown in vitro:
(A) Reductase
(B) Hydrolase
(C) Ligase
(D) Oxidase
121. Increased serum alanine during fasting is due to
(A) Breakdown of muscle proteins
(B) Decreased utilization of non essential amino acids
(C) Leakage of aminoacids to plasma
(D) Impaired renal function
122. The following 4 amino acids are required for completion
of urea cycle except
(A) Aspartic acid
(B) Arginine
(C) Ornithine
(D) Glycine
123. Number of amino acids present in the dietary proteins:
(A) 22
(B) 23
(C) 20
(D) 19
124. Urea synthesis takes place in
(A) Blood
(B) Liver
(C) Kidney
(D) Heart
125. All followings are ketogenic aminoacids except
(A) Leucine
(B) Isoleucine
(C) Phenyl alanine
(D) Glycine
126. The amino acid containing an indole ring:
(A) Tryptophan
(B) Arginine
(C) Threonine
(D) Phenylalanine
127. Histidine is converted to histamine through the process
of
(A) Transamination
(B) Decarboxylation
(C) Oxidative deamination
(D) Urea cycle
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