In Lineweaver-Burk plot, the y-intercept represents (A) Vmax (B) Km (C) Km (D) 1/Km

In Lineweaver-Burk plot, the y-intercept represents (A) Vmax (B) Km (C) Km (D) 1/Km
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Answer :  B
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Kinetics of an allosteric enzyme are explained by (A) Michaelis-Menten equation (B) Lineweaver-Burk plot (C) Hill plot (D) All of these

Description : Kinetics of an allosteric enzyme are explained by (A) Michaelis-Menten equation (B) Lineweaver-Burk plot (C) Hill plot (D) All of these

Last Answer : Answer : C

Lineweaver – Burk double reciprocal plot is related to (A) Substrate concentration (B) Enzyme activity (C) Temperature (D) Both (A) and (B) ENZYMES 145

Description : Lineweaver – Burk double reciprocal plot is related to (A) Substrate concentration (B) Enzyme activity (C) Temperature (D) Both (A) and (B) ENZYMES 145

Last Answer : Answer : D

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

Description : 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

Last Answer : Answer : C

Which of the following statements about an enzyme exhibiting allosteric kinetics with cooperative interaction is false? (A) A plot of V-Vk [s] has a sigmaidal shape (B) An inhibitor may increase the apparent Km (C) Line weaver Bnrk plot is useful for determining Km and Vmax (D) Removal of allosteric inhibitor may result in hyperbolic V-S [s] plot

Description : Which of the following statements about an enzyme exhibiting allosteric kinetics with cooperative interaction is false? (A) A plot of V-Vk [s] has a sigmaidal shape (B) An inhibitor may increase the ... Km and Vmax (D) Removal of allosteric inhibitor may result in hyperbolic V-S [s] plot

Last Answer : Answer : D

The following abnormality in PRPP synthetase can cause primary gout: (A) High Vmax (B) Low Km (C) Resistance to allosteric inihbition. (D) All of these

Description : The following abnormality in PRPP synthetase can cause primary gout: (A) High Vmax (B) Low Km (C) Resistance to allosteric inihbition. (D) All of these

Last Answer : Answer : D

Km value of enzyme is substrate concentration at (A) ½ Vmax (B) 2 Vmax (C) ½ Vmax (D) 4 Vmax

Description : Km value of enzyme is substrate concentration at (A) ½ Vmax (B) 2 Vmax (C) ½ Vmax (D) 4 Vmax

Last Answer : Answer : D

The presence of a non competitive inhibitor (A) Leads to both an increase in the Vmax of a reaction and an increase in Km (B) Leads to a decrease in the observed Vmax (C) Leads to a decrease in Km and Vmax (D) Leads to an increase in Km without affecting Vmax

Description : The presence of a non competitive inhibitor (A) Leads to both an increase in the Vmax of a reaction and an increase in Km (B) Leads to a decrease in the observed Vmax (C) Leads to a decrease in Km and Vmax (D) Leads to an increase in Km without affecting Vmax

Last Answer : Answer : B

The rate of an enzyme catalyzed reaction was measured using several substrate concentrations that were much lower than Km, the dependence of reaction velocity on substrate concentration can best be described as (A) Independent of enzyme concentration (B) A constant fraction of Vmax (C) Equal to Km (D) Proportional to the substrate concentration

Description : The rate of an enzyme catalyzed reaction was measured using several substrate concentrations that were much lower than Km, the dependence of reaction velocity on substrate concentration can best be ... constant fraction of Vmax (C) Equal to Km (D) Proportional to the substrate concentration

Last Answer : Answer : C

The Michaelis constant, Km is (A) Numerically equal to ½ Vmax (B) Dependent on the enzyme concentration (C) Independent of pH (D) Numerically equal to the substrate concentration that gives half maximal velocity

Description : The Michaelis constant, Km is (A) Numerically equal to ½ Vmax (B) Dependent on the enzyme concentration (C) Independent of pH (D) Numerically equal to the substrate concentration that gives half maximal velocity

Last Answer : Answer : D

A competitive inhibitor of an enzyme (A) Increases Km without affecting Vmax (B) Decreases Km without affecting Vmax (C) Increases Vmax without affecting Km (D) Decreases both Vmax and Km

Description : A competitive inhibitor of an enzyme (A) Increases Km without affecting Vmax (B) Decreases Km without affecting Vmax (C) Increases Vmax without affecting Km (D) Decreases both Vmax and Km

Last Answer : Answer : A

In competitive inhibition which of the following kinetic effect is true ? (A) Decreases both Km and Vmax (B) Increases both Km and Vmax (C) Decreases Km without affecting Vmax (D) Increases Km without affecting Vmax

Description : In competitive inhibition which of the following kinetic effect is true ? (A) Decreases both Km and Vmax (B) Increases both Km and Vmax (C) Decreases Km without affecting Vmax (D) Increases Km without affecting Vmax

Last Answer : Answer : D

In competitive inhibition of enzyme action (A) The apparent Km is decreased (B) The apparent Km is increased (C) Vmax is decreased (D) Apparent concentration of enzyme molecules decreased

Description : In competitive inhibition of enzyme action (A) The apparent Km is decreased (B) The apparent Km is increased (C) Vmax is decreased (D) Apparent concentration of enzyme molecules decreased

Last Answer : Answer : B

When [s] is equal to Km, which of the following conditions exist? (A) Half the enzyme molecules are bound to substrate (B) The velocity of the reaction is equal to Vmax (C) The velocity of the reaction is independent of substrate concentration (D) Enzyme is completely saturated with substrate

Description : When [s] is equal to Km, which of the following conditions exist? (A) Half the enzyme molecules are bound to substrate (B) The velocity of the reaction is equal to Vmax (C) The velocity of the reaction is independent of substrate concentration (D) Enzyme is completely saturated with substrate

Last Answer : Answer : A

In non-competitive enzyme action (A) Vmax is increased (B) Apparent km is increased (C) Apparent km is decreased (D) Concentration of active enzyme molecule is reduced

Description : In non-competitive enzyme action (A) Vmax is increased (B) Apparent km is increased (C) Apparent km is decreased (D) Concentration of active enzyme molecule is reduced

Last Answer : Answer : C

If the substrate concentration is much below the km of the enzyme, the velocity of the reaction is (A) Directly proportional to substrate concentration (B) Not affected by enzyme concentration (C) Nearly equal to Vmax (D) Inversely proportional to substrate concentration

Description : If the substrate concentration is much below the km of the enzyme, the velocity of the reaction is (A) Directly proportional to substrate concentration (B) Not affected by enzyme concentration (C) Nearly equal to Vmax (D) Inversely proportional to substrate concentration

Last Answer : Answer : A

Competitive inhibitors (A) Decrease the Km (B) Decrease the Vmax (C) Increase the Km (D) Increase the Vmax

Description : Competitive inhibitors (A) Decrease the Km (B) Decrease the Vmax (C) Increase the Km (D) Increase the Vmax

Last Answer : Answer : C

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

Description : 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

Last Answer : Answer : D

In competitive enzyme activity inhibition (A) Apparent Km is decreased (B) Apparent Km is increased (C) Vmax is increased (D) Vmax is decreased

Description : In competitive enzyme activity inhibition (A) Apparent Km is decreased (B) Apparent Km is increased (C) Vmax is increased (D) Vmax is decreased

Last Answer : Answer : B

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

Description : 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

Last Answer : Answer : A

In competitive enzyme activity inhibition (A) The structure of inhibitor generally resembles that of the substrate (B) Inhibitor decreases apparent Km (C) Km remains unaffective (E) Inhibitor decreases Vmax without affecting Km

Description : In competitive enzyme activity inhibition (A) The structure of inhibitor generally resembles that of the substrate (B) Inhibitor decreases apparent Km (C) Km remains unaffective (E) Inhibitor decreases Vmax without affecting Km

Last Answer : Answer : A

In reversible non-competitive enzyme activity inhibition (A) Vmax is increased (B) Km is increased (C) Km is decreased (D) Concentration of active enzyme is reduced

Description : In reversible non-competitive enzyme activity inhibition (A) Vmax is increased (B) Km is increased (C) Km is decreased (D) Concentration of active enzyme is reduced

Last Answer : Answer : D

The kinetic effect of purely competitive inhibitor of an enzyme (A) Increases Km without affecting Vmax (B) Decreases Km without affecting Vmax (C) Increases Vmax without affecting Km (D) Decreases Vmax without affecting Km

Description : The kinetic effect of purely competitive inhibitor of an enzyme (A) Increases Km without affecting Vmax (B) Decreases Km without affecting Vmax (C) Increases Vmax without affecting Km (D) Decreases Vmax without affecting Km

Last Answer : Answer : A

Pick out the wrong statement. (A) A particular chemical reaction is more temperature sensitive at low temperatures (B) A very high value of equilibrium constant, K (K >> 1) indicates that the reaction is practically irreversible in nature (C) The intercept of the Arrhenius plot is called the 'activation energy' (D) Non-ideal flow takes place in reactors due to recycling, channeling or by creation of stagnant regions

Description : Pick out the wrong statement. (A) A particular chemical reaction is more temperature sensitive at low temperatures (B) A very high value of equilibrium constant, K (K >> 1) indicates that the ... ) Non-ideal flow takes place in reactors due to recycling, channeling or by creation of stagnant regions

Last Answer : (C) The intercept of the Arrhenius plot is called the 'activation energy

Pick out the wrong statement. (A) Use of different catalysts in a reversible catalytic chemical reaction does not change the equilibrium composition (B) Alumina is added as a promoter to iron catalyst in ammonia synthesis reaction (C) Activation energy for a reaction is obtained from the intercept of the Arrhenius plot (D) Presence of inerts affects the equilibrium conversion of reactants in a chemical reaction

Description : Pick out the wrong statement. (A) Use of different catalysts in a reversible catalytic chemical reaction does not change the equilibrium composition (B) Alumina is added as a promoter to ... Arrhenius plot (D) Presence of inerts affects the equilibrium conversion of reactants in a chemical reaction

Last Answer : (C) Activation energy for a reaction is obtained from the intercept of the Arrhenius plot

A competitive inhibitor of an enzyme has which of the following properties? (A) It is frequently a feedback inhibitor (B) It becomes covalently attached to an enzyme (C) It decreases the Vmax (D) It interferes with substrate binding to the enzyme

Description : A competitive inhibitor of an enzyme has which of the following properties? (A) It is frequently a feedback inhibitor (B) It becomes covalently attached to an enzyme (C) It decreases the Vmax (D) It interferes with substrate binding to the enzyme

Last Answer : Answer : D

Vmax of an enzyme may be affected by (A) pH (B) Temperature (C) Non-competitive inhibitors (D) All of these

Description : Vmax of an enzyme may be affected by (A) pH (B) Temperature (C) Non-competitive inhibitors (D) All of these

Last Answer : Answer : D

In enzyme kinetics Vmax reflects (A) The amount of an active enzyme (B) Substrate concentration (C) Half the substrate concentration (D) Enzyme substrate complex

Description : In enzyme kinetics Vmax reflects (A) The amount of an active enzyme (B) Substrate concentration (C) Half the substrate concentration (D) Enzyme substrate complex

Last Answer : Answer : A

What is the equation of the line having the y-intercept –1 and parallel to the line y = 5x – 7 ? -Maths 9th

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Last Answer : Slope of AB = \(rac{2-4}{1-0}\) = -2, Slope of BC = \(rac{3-2}{3-1}\) = \(rac{1}{2}\)Slope of AC = \(rac{3-4}{3-0}\) = \(-rac{1}{3}\)Slope of AB × Slope of BC = -2 x \(rac{1}{2}\) = -1∴ AB ⊥ BC, i.e, ∠B = 90º ⇒ ΔABC is a right angled.

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Last Answer : (a) 4x + 3y = 24 Let the x-intercept = a. Then, y-intercept = 14 - a ∴ Eqn of the straight line is \(rac{x}{a}\) + \(rac{y}{14-a}\) = 1Since it passes through (3, 4), so\(rac{3}{a}\) + \(rac{4}{14-a}\) = 1⇒ 3(14 - ... = 1 ⇒ x + y = 7or \(rac{x}{6}\) + \(rac{y}{8}\) = 1 ⇒ 8x + 6y = 48 ⇒ 4x + 3y = 24.

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