InterviewSolution
This section includes InterviewSolutions, each offering curated multiple-choice questions to sharpen your knowledge and support exam preparation. Choose a topic below to get started.
| 251. |
Which of the following is a microsomal enzyme inducer? (A) Indomethacin (B) Clofibrate (C) Tolbutamide (D) Glutethamide |
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Answer» (D) Glutethamide |
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| 252. |
What is meant by substrates of enzymatic reactions? |
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Answer» Substrates are reagent molecules upon which enzymes act. The enzyme has spatial binding sites for the attachment of its substrate. These sites are called activation centres of the enzyme. Substrates bind to theses centres forming the enzyme-substrate complex. |
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| 253. |
From the L ineweaver-Burk p lot of Michaelis-Menten equation, Km and Vmax can be determined when V is the reaction velocity at substrate concentration S, the X-axis experimental data are expressed as (A) 1/V (B) V (C) 1/S (D) S |
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Answer» The X-axis experimental data are expressed as 1/S. |
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| 254. |
A sigmoidal plot of substrate concentration ([S]) verses reaction velocity (V) may indicate (A) Michaelis-Menten kinetics (B) Co-operative binding (C) Competitive inhibition (D) Non-competitive inhibition |
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Answer» (B) Co-operative binding |
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| 255. |
ATP is a co-substrate as well as an allosteric inhibitor of (A) Phosphofructokinase (B) Hexokinase (C) Glucokinase (D) None of these |
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Answer» (A) Phosphofructokinase |
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| 256. |
A/G ratio is(A) Strength of proteins(B) Ratio of serum proteins(C) Ratio of ceruloplasmin(D) None of these |
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Answer» Correct option is (B) Ratio of serum proteins A/G ratio is the (B) Ratio of serum proteins. It is simply the ratio of albumin to globulin. |
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| 257. |
A demonstrable inducer is absent in (A) Allosteric enzyme (B) Constitutive enzyme (C) Inhibited enzyme (D) Co-operative enzyme |
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Answer» (B) Constitutive enzyme |
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| 258. |
Concerning enzymatic reactions, how different are the graphic curve of the variation of the speed of a reaction as function of substrate concentration and the curve of variation of the speed of a reaction as function of temperature? |
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Answer» The curve of variation of speed of the enzymatic reaction as a function of growing substrate concentration is a growing curve until the point where it stabilizes due to the saturation of the activation centres of the enzymes. The curve of variation of speed of the enzymatic reaction as a function of growing temperature has a crescent portion and reaches a peak (the optimum temperature) then it decreases and reaches zero in the point of inactivity of the enzymes by denaturation. |
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| 259. |
How is the cooling of organs and tissues for medical transplants associated with the effect of temperature upon enzymatic reactions? |
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Answer» The molecular degradation during the decomposition of organs and tissues is catalyzed by enzymes. The cooling to adequate temperatures of some organs and tissues destined for transplantation reduces that enzyme activity and thus lessens the natural decomposition process. By the same rationale, the cooling reduces the metabolic work of cells and prevents the degradation of their own structures to obtain energy. Elevation of temperature later reverts denaturation of enzymes and the organs and tissues also preserved by other specific techniques may be grafted into the receptors. |
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| 260. |
In enzyme kinetics Km implies (A) The substrate concentration that gives one half Vmax (B) The dissocation constant for the enzyme substrate comples (C) Concentration of enzyme (D) Half of the substrate concentration required to achieve Vmax |
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Answer» (A) The substrate concentration that gives one half Vmax |
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| 261. |
An allosteric enzyme is generally inhibited by (A) Initial substrate of the pathway (B) Substrate analogues (C) Product of the reaction catalysed by allosteric enzyme (D) Product of the pathway |
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Answer» (D) Product of the pathway |
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| 262. |
In Lineweaver-Burk plot, the y-intercept represents (A) Vmax (B) Km (C) Km (D) 1/Km |
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Answer» In Lineweaver-Burk plot, the y-intercept represents Km. |
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| 263. |
In enzyme kinetics Vmax reflects (A) The amount of an active enzyme (B) Substrate concentration (C) Half the substrate concentration (D) Enzyme substrate complex |
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Answer» (A) The amount of an active enzyme |
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| 264. |
When the velocity of an enzymatic reaction equals Vmax, substrate concentration is (A) Half of Km (B) Equal to Km (C) Twice the Km (D) Far above the Km |
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Answer» (D) Far above the Km |
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| 265. |
For the enzymatic reaction what is the effect of a substance with the same spatial conformation as an enzymatic substrate? How is this type of substance known? |
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Answer» Substances that “simulate” substrates can bind to the activation centre of enzymes thus blocking the true substrates to bind to these enzymes and paralyzing the enzymatic reaction. Such “fake substrates” are called enzyme inhibitors. The binding of enzyme inhibitors to enzymes can be reversible or irreversible. Many medical drugs, for example, some antibiotics, antivirals, antineoplastics, antihypertensives and even sildenafil (trade name Viagra), are enzyme inhibitors that block enzyme activity. |
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| 266. |
How does the substrate concentration affect the speed of enzymatic reactions? |
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Answer» Initially as substrate concentration increases, the speed of the reaction increases; this happens because free activation centres of the enzyme bind to free substrates. Once all activation centres of the available enzymes become bound to their substrates new increments of the substrate concentration will have no effect on the speed of the reaction. |
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| 267. |
The energy required to start an enzymatic reaction is called (A) Chemical energy (B) Metabolic energy (C) Activation energy (D) Potential energy |
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Answer» (C) Activation energy |
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| 268. |
Feedback term refers to (A) Effect of substrate on rate of enzymatic reaction (B) Effect of end product on rate reaction (C) Effect of enzyme concentration on rate of reaction (D) Effect of external compound on rate of reaction |
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Answer» (B) Effect of end product on rate reaction |
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| 269. |
A protein having both structural and enzymatic traits is (A) Myosin (B) Collagen (C) Trypsin (D) Actin |
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Answer» A protein having both structural and enzymatic traits is Myosin. |
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| 270. |
Why can it be said that the enzymatic action is highly specific? |
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Answer» The enzymatic action is highly specific because only specific substrates of one enzyme bind to the activation centre of that enzyme. Each enzyme generally catalyzes only a specific chemical reaction. |
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| 271. |
Enzymes activity is controlled by (A) pH of the solution (B) Temperature (C) Concentration of the enzyme (D) Concentration of the substrate (E) All of these |
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Answer» (C) Concentration of the enzyme |
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| 272. |
Which of the following statements is true? (A) Enzymes have names ending ase (B) Enzymes are highly specific in their action (C) Enzymes are living organisms (D) Enzymes get activated on heating |
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Answer» (B) Enzymes are highly specific in their action |
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| 273. |
Genetic engineering requires enzyme: (A) DNA ase (B) Amylase (C) Lipase (D) Restriction endonuclease |
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Answer» (D) Restriction endonuclease |
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| 274. |
In biosynthesis of cholesterol triparanol inhibits the activity of the enzyme: (A) ∆24 Reductase (B) Oxidosqualene-lanosterol cyclase (C) Isomerase (D) Squalene epoxidase |
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Answer» (A) ∆24 Reductase |
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| 275. |
One of the enzymes regulating glycolysis is (A) Phosphofructokinase (B) Glyceraldehyde-3-phosphate dehydrogenase (C) Phosphotriose isomerase (D) Phosphohexose isomerase |
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Answer» (A) Phosphofructokinase |
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| 276. |
In glycolytic pathway, iodacetate inhibits the activity of the enzyme: (A) Phosphotriose isomerase (B) Glyceraldehyde-3-phosphate dehydrogenase (C) Pyruvate kinase (D) Phosphofructokinase |
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Answer» (B) Glyceraldehyde-3-phosphate dehydrogenase |
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| 277. |
Enzyme catalyzed hydrolysis of proteins produces amino acid of the form (A) D (B) DL (C) L (D) Racemic |
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Answer» Enzyme catalyzed hydrolysis of proteins produces amino acid of the form L. |
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| 278. |
What are catalysts? |
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Answer» Catalysts are substances that reduce the activation energy of a chemical reaction, facilitating it or making it energetically viable. The catalyst increases the speed of the chemical reaction. |
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| 279. |
Is there a difference between the initial and the final energy levels in catalyzed and non-catalyzed reactions? |
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Answer» The catalysis does not alter the energetic state of reagents and products of a chemical reaction. Only the energy necessary for the reaction to occur, i.e., the activation energy is altered. |
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| 280. |
What amount of catalyst is consumed in the reaction it catalyzes? |
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Answer» Catalysts are not consumed in the reactions they catalyze. |
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| 281. |
Tryptophan pyrolase is currently known as (A) Tryptophan deaminase (B) Tryptophan dioxygenase (C) Tryptophan mono oxygenase (D) Tryptophan decarboxylase |
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Answer» (B) Tryptophan dioxygenase |
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| 282. |
In the normal resting state of human most of the blood glucose burnt as fuel is consumed by (A) Liver (B) Brain (C) Adipose tissue (D) Muscles |
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Answer» The Correct option is (B) Brain |
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| 283. |
In normal individuals glycosuria occurs when the venous blood glucose concentration exceeds (A) 5–6 mmol/L (B) 7–8 mmol/L (C) 8.5–9 mmol/L (D) 9.5–10 mmol/L |
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Answer» (A) 5–6 mmol/L |
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| 284. |
Homogentisic oxidase is an (A) Oxidase (B) Monooxygenase (C) Dioxygenase (D) Anaerotic dehydrogenase |
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Answer» (C) Dioxygenase |
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| 285. |
Mitochondrial membrane is freely preamble to (A) Pyruvate (B) Malate (C) Oxaloacetate (D) Fumarate |
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Answer» Mitochondrial membrane is freely preamble to malate. |
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| 286. |
The enzyme regulating extramitochondrial fatty acid synthesis is (A) Thioesterase (B) Acetyl CoA carboxylase (C) Acyl transferase (D) Multi-enzyme complex |
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Answer» (B) Acetyl CoA carboxylase |
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| 287. |
Renal glycosuria is characterized by (A) Hyperglycemia (B) Hyperglycemia with glycosuria (C) Normal blood glucose level with glycosuria (D) Hyperglycemia with ketosis |
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Answer» (C) Normal blood glucose level with glycosuria |
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| 288. |
Isocitrate dehydrogenase can use __________ as a cofactor. (A) NAD+ only (B) NADP+ only (C) NAD+ or NADP+ (D) FMN and FAD |
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Answer» Isocitrate dehydrogenase can use NAD+ or NADP+ as a cofactor. |
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| 289. |
The enzymes of the citric acid cycle are located in (A) Mitochondrial matrix (B) Extramitochondrial soluble fraction of the cell (C) Nucleus (D) Endoplasmic reticulum |
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Answer» (A) Mitochondrial matrix |
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| 290. |
In anaerobic glycolysis, energy yield from each molecule of glucose is (A) 2 ATP equivalents (B) 8 ATP equivalents (C) 30 ATP equivalents(D) 38 ATP equivalents |
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Answer» (A) 2 ATP equivalents |
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| 291. |
The main source of reducing equivalents (NADPH) for lipogenesis is (A) Pentose phosphate pathway (B) Citric acid cycle (C) Glycolysis (D) Glycogenolysis |
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Answer» (A) Pentose phosphate pathway |
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| 292. |
Lactate dehydrogenase is a (A) Monomer (B) Dimer (C) Tetramer (D) Hexamer |
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Answer» Lactate dehydrogenase is a Tetramer. |
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| 293. |
Higher rate of lipogenesis is associated with (A) High proportion of carbohydrate in diet (B) Restricted caloric intake (C) High fat diet (D) Deficiency of insulin |
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Answer» (A) High proportion of carbohydrate in diet |
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| 294. |
Phlorizin inhibits (A) Renal tubular reabsorption of glucose (B) Glycolysis (C) Gluconeogenesis (D) Glycogenolysis |
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Answer» (A) Renal tubular reabsorption of glucose |
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| 295. |
Ceruloplasmin oxidizes (A) Copper (B) Iron (C) Both (A) and (B) (D) None of these |
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Answer» (C) Both (A) and (B) |
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| 296. |
The principal rate limiting step in the biosynthesis of bile acids is at the (A) 7-Hydroxylase reaction (B) 12 α-Hydroxylase reaction (C) Conjugation reaction (D) Deconjugation reaction |
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Answer» (A) 7-Hydroxylase reaction |
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| 297. |
Ceruloplasmin is absent in (A) Cirrhosis of liver (B) Wilson’s disease (C) Menke’s disease (D) Copper deficiency |
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Answer» (B) Wilson’s disease |
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| 298. |
In the reaction below, Nu TP stands for NuTP + glucose → Glucose 6–Phosphate + NuDP. (A) ATP (B) CTP (C) GTP (D) UTP |
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Answer» The Correct option is (A) ATP |
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| 299. |
Farber’s disease is due to the deficiency of the enzyme: (A) α-Galactosidase (B) Ceramidase (C) β-Glucocerebrosidase (D) Arylsulphatase A. |
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Answer» (B) Ceramidase |
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| 300. |
Fabry’s disease is due to the deficiency of the enzyme: (A) Ceramide trihexosidase (B) Galactocerebrosidase (C) Phytanic acid oxidase (D) Sphingomyelinase |
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Answer» (A) Ceramide trihexosidase |
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