The correct answer is (1) iv. Affinity chromatography. Introduction Enzyme purification is a multistep process designed to isolate proteins from complex biological mixtures. Each stage serves to increase the purity and […]
Tag: csir enzymes kinetics PYQ
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CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Mechanism of Enzyme Degradation by the 26S Proteasome: Orientation of Active Sites and Ubiquitin Targeting
(NOV 2020-11) 77. In regulating the quantity of enzyme, its degradation plays a pivotal role. Following statements are made to represent the degradation of enzymes in the 26S proteasome. A. […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Calculating Enzyme Velocity with Competitive Inhibition: A Practical Example
(SEPT 2022-11) 72. An enzyme has a Km of 5 x 10-5 M and a Vmax of 100 µmoles.lit-1. min-1(Km is the Michaelis constant and Vmax is the maximal velocity). […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Uncompetitive Enzyme Inhibition: Binding Mechanism and Effects on KmKm and VmaxVmax
(FEB 2022-1) 71. Following statements are made about uncompetitive inhibition of an enzyme: A. Uncompetitive inhibitor binds to both free enzyme as well as an enzyme- substrate complex. B. Addition […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Uncompetitive Inhibition: Effects on Enzyme Kinetics and Determination of Km and Vmax
(DEC 2012) 70. An enzyme catalyzed reaction was measured in the presence and absence of an inhibitor for an uncompetitive inhibition, (1) only Km is increased (2) only is Vmax […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Demystifying Competitive Enzyme Inhibition: Substrate Competition and Reversibility
(DEC 2013 GU) 69. If the product of an enzyme binds to the enzyme- substrate complex to exhibit its activity through a decrease in both Km and Vmax, this type […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Lineweaver-Burk Plot Analysis for Km Determination in Reversible Non-Competitive Enzyme Inhibition
The correct answer is (1). Introduction Enzyme inhibition is a cornerstone of biochemistry and pharmacology, and visualizing its effects on kinetic parameters is essential. The Lineweaver-Burk double reciprocal plot provides a […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Non-Competitive Enzyme Inhibition: Effects on Kinetic Parameters VmaxVmax and KmKm
(JUNE 2002) 66. Which of following is true for non-competitive inhibition? (1) Increases Vmax (2) Decreases Vmax (3) Increases Km (4) Decreases Km The correct answer is (2) Decreases Vmax. Introduction […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Noncompetitive Enzyme Inhibition: Reaction Schemes, Mechanism, and Impact on Kinetics
The correct answer is (2) E+S ⇄ ES → E+P; ES+I ⇄ ESI. Introduction Noncompetitive inhibition is a fundamental model in enzyme kinetics, describing how inhibitors can reduce enzyme activity regardless […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Understanding Competitive Inhibition: How Substrate Concentration Overcomes Inhibition
(DEC 2001) 64. False statement of competitive inhibition is- (1) Structure same as substrate (2) Inhibits substrate binding (3) Binds to active site (4) Reaction cannot be favorably biased by […]
