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

From the L ineweaver-Burk p lot of Michaelis-Menten equation, Km and V

1.	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
Answer» The X-axis experimental data are expressed as 1/S.

Discussion

No Comment Found

Related InterviewSolutions

Cyclic AMP binds to (A) Catalytic subunits of protein kinase (B) Regulatory subunits of protein kinase (C) Catalytic subunits of phosphorylase kinase (D) Regulatory subunits of phosphorylase kinase
Feedback inhibition of enzyme is influenced by (A) Enzyme (B) External factors (C) End product (D) Substrate
At low blood glucose concentration, brain but not liver will take up glucose. It is due to the (A) Low Km of hexokinase (B) Low Km of glucokinase (C) Specificity of glucokinase (D) Blood brain barrier
Since pepsin is a gastric enzyme does it have an acid or basic optimum pH? What happens to pepsin when it passes into the duodenum?
Template/lock and key theory of enzyme action is supported by (A) Enzymes speed up reaction (B) Enzymes occur in living beings and speed up certain reactions (C) Enzymes determine the direction of reaction (D) Compounds similar to substrate inhibit enzyme activity
Fischer’s ‘lock and key’ model of the enzyme action implies that (A) The active site is complementary in shape to that of substance only after interaction. (B) The active site is complementary in shape to that of substance (C) Substrates change conformation prior to active site interaction (D) The active site is flexible and adjusts to substrate
Glycolysis is anaerobic in (A) Liver (B) Brain (C) Kidneys (D) Erythrocytes
‘Lock’ and ‘Key’ theory was proposed by(A) Sorenson(B) Fischer(C) Mehler(D) Sanger
Which of the following enzymes incorporates inorganic phosphate into the substrate? (A) Phosphoglycerate kinase (B) Glyceraldehyde-3-phosphate dehydrogenase (C) Pyruvate kinase (D) Enolase
In erythrocytes, 2, 3-biphosphoglycerate is derived from the intermediate: (A) Glyeraldehyde-3-phosphate (B) 1, 3-Biphosphoglycerate (C) 3-Phosphoglycerate (D) 2-Phosphoglycerate

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

Discussion

No Comment Found

Related InterviewSolutions

Reply to Comment