(a) Interpretation: V 0 versus pH curve when the substrate concentration is much greater than the enzyme K M should be drawn. Concept introduction: K M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K M needs a higher concentration of substrate to achieve V max .

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Answer 1

Question

Chapter 8, Problem 46P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

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a) What are the differences between the Direct & Indirect Immunofluorescence Assays? (0.5 mark) b) What are the advantages of the Indirect Immunofluorescence Assays? (0.5 mark) c) A Super-Resolution Imaging Technique was developed in 2018 using imidazole, a His-tag ligand conjugated with a fluorophore to report the presence of a recombinant His-tag protein target, (Sci Rep, 2018, 8:5507). How does this technique improve the image quality? (2 marks)

a) What are the differences between the Direct & Indirect Immunofluorescence Assays? b) What are the advantages of the Indirect Immunofluorescence Assays? c) A Super-Resolution Imaging Technique was developed in 2018 using imidazole, a His-tag ligand conjugated with a fluorophore to report the presence of a recombinant His-tag protein target, (Sci Rep, 2018, 8:5507). How does this technique improve the image quality?

Answer 2

Question

Chapter 8, Problem 46P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

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Answer 3

Question

Chapter 8, Problem 46P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

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Answer 4

Question

Chapter 8, Problem 46P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

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Answer 5

Chapter 8, Problem 46P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 6

Chapter 8, Problem 46P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 7

Chapter 8, Problem 46P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 8

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 9

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 10

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 11

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 12

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Answer 13

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Answer 14

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Answer 15

Ch. 8 - Prob. 1P Ch. 8 - Prob. 2P Ch. 8 - Prob. 3P Ch. 8 - Prob. 4P Ch. 8 - Prob. 5P Ch. 8 - Prob. 6P Ch. 8 - Prob. 7P Ch. 8 - Prob. 8P Ch. 8 - Prob. 9P Ch. 8 - Prob. 10P

Solution Summary: The author explains the Michaelis constant, which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system.

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Chapter 8 Solutions