The reason that certain protein has an apparent molecular mass of 90KD when determined by the gel filtration and 60kD when determined by SDS-PAGE in the presence or absence of 2-mercaptoethanol. Concept introduction: Gel filtration is a technique used for the separation of molecules based on the molecular size. In these techniques, molecules move through the porous of beads, diffusing into the beads with greater or lesser degrees of interaction. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analyzes the protein mixture based on size. Proteins that have higher and lower molecular mass run slowly and fast in the gel under the effect of an electric field respectively.

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Answer 1

Question

Chapter 5, Problem 9E

Summary Introduction

To explain: The reason that certain protein has an apparent molecular mass of 90KD when determined by the gel filtration and 60kD when determined by SDS-PAGE in the presence or absence of 2-mercaptoethanol.

Concept introduction: Gel filtration is a technique used for the separation of molecules based on the molecular size. In these techniques, molecules move through the porous of beads, diffusing into the beads with greater or lesser degrees of interaction. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analyzes the protein mixture based on size. Proteins that have higher and lower molecular mass run slowly and fast in the gel under the effect of an electric field respectively.

Summary Introduction

To determine: Whether gel filtration or SDS-PAGE would be accurate to find molecular mass of proteins.

Concept introduction: Gel filtration is a technique used for the separation of molecules based on the molecular size. In these techniques, molecules move through the porous of beads, diffusing into the beads with greater or lesser degrees of interaction. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analyzes the protein mixture based on size. Proteins that have higher and lower molecular mass run slowly and fast in the gel under the effect of an electric field respectively.

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Answer 2

Question

Chapter 5, Problem 9E

Summary Introduction

To explain: The reason that certain protein has an apparent molecular mass of 90KD when determined by the gel filtration and 60kD when determined by SDS-PAGE in the presence or absence of 2-mercaptoethanol.

Concept introduction: Gel filtration is a technique used for the separation of molecules based on the molecular size. In these techniques, molecules move through the porous of beads, diffusing into the beads with greater or lesser degrees of interaction. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analyzes the protein mixture based on size. Proteins that have higher and lower molecular mass run slowly and fast in the gel under the effect of an electric field respectively.

Summary Introduction

To determine: Whether gel filtration or SDS-PAGE would be accurate to find molecular mass of proteins.

Concept introduction: Gel filtration is a technique used for the separation of molecules based on the molecular size. In these techniques, molecules move through the porous of beads, diffusing into the beads with greater or lesser degrees of interaction. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analyzes the protein mixture based on size. Proteins that have higher and lower molecular mass run slowly and fast in the gel under the effect of an electric field respectively.

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Answer 3

Question

Chapter 5, Problem 9E

Summary Introduction

To explain: The reason that certain protein has an apparent molecular mass of 90KD when determined by the gel filtration and 60kD when determined by SDS-PAGE in the presence or absence of 2-mercaptoethanol.

Concept introduction: Gel filtration is a technique used for the separation of molecules based on the molecular size. In these techniques, molecules move through the porous of beads, diffusing into the beads with greater or lesser degrees of interaction. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analyzes the protein mixture based on size. Proteins that have higher and lower molecular mass run slowly and fast in the gel under the effect of an electric field respectively.

Summary Introduction

To determine: Whether gel filtration or SDS-PAGE would be accurate to find molecular mass of proteins.

Concept introduction: Gel filtration is a technique used for the separation of molecules based on the molecular size. In these techniques, molecules move through the porous of beads, diffusing into the beads with greater or lesser degrees of interaction. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analyzes the protein mixture based on size. Proteins that have higher and lower molecular mass run slowly and fast in the gel under the effect of an electric field respectively.

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Answer 4

Question

Chapter 5, Problem 9E

Summary Introduction

To explain: The reason that certain protein has an apparent molecular mass of 90KD when determined by the gel filtration and 60kD when determined by SDS-PAGE in the presence or absence of 2-mercaptoethanol.

Concept introduction: Gel filtration is a technique used for the separation of molecules based on the molecular size. In these techniques, molecules move through the porous of beads, diffusing into the beads with greater or lesser degrees of interaction. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analyzes the protein mixture based on size. Proteins that have higher and lower molecular mass run slowly and fast in the gel under the effect of an electric field respectively.

Summary Introduction

To determine: Whether gel filtration or SDS-PAGE would be accurate to find molecular mass of proteins.

Concept introduction: Gel filtration is a technique used for the separation of molecules based on the molecular size. In these techniques, molecules move through the porous of beads, diffusing into the beads with greater or lesser degrees of interaction. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analyzes the protein mixture based on size. Proteins that have higher and lower molecular mass run slowly and fast in the gel under the effect of an electric field respectively.

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Answer 5

Chapter 5, Problem 9E

Summary Introduction

To explain: The reason that certain protein has an apparent molecular mass of 90KD when determined by the gel filtration and 60kD when determined by SDS-PAGE in the presence or absence of 2-mercaptoethanol.

Concept introduction: Gel filtration is a technique used for the separation of molecules based on the molecular size. In these techniques, molecules move through the porous of beads, diffusing into the beads with greater or lesser degrees of interaction. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analyzes the protein mixture based on size. Proteins that have higher and lower molecular mass run slowly and fast in the gel under the effect of an electric field respectively.

Summary Introduction

To determine: Whether gel filtration or SDS-PAGE would be accurate to find molecular mass of proteins.

Concept introduction: Gel filtration is a technique used for the separation of molecules based on the molecular size. In these techniques, molecules move through the porous of beads, diffusing into the beads with greater or lesser degrees of interaction. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analyzes the protein mixture based on size. Proteins that have higher and lower molecular mass run slowly and fast in the gel under the effect of an electric field respectively.

Answer 6

Chapter 5, Problem 9E

Summary Introduction

To explain: The reason that certain protein has an apparent molecular mass of 90KD when determined by the gel filtration and 60kD when determined by SDS-PAGE in the presence or absence of 2-mercaptoethanol.

Concept introduction: Gel filtration is a technique used for the separation of molecules based on the molecular size. In these techniques, molecules move through the porous of beads, diffusing into the beads with greater or lesser degrees of interaction. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analyzes the protein mixture based on size. Proteins that have higher and lower molecular mass run slowly and fast in the gel under the effect of an electric field respectively.

Answer 7

Chapter 5, Problem 9E

Summary Introduction

To explain: The reason that certain protein has an apparent molecular mass of 90KD when determined by the gel filtration and 60kD when determined by SDS-PAGE in the presence or absence of 2-mercaptoethanol.

Concept introduction: Gel filtration is a technique used for the separation of molecules based on the molecular size. In these techniques, molecules move through the porous of beads, diffusing into the beads with greater or lesser degrees of interaction. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analyzes the protein mixture based on size. Proteins that have higher and lower molecular mass run slowly and fast in the gel under the effect of an electric field respectively.

Answer 8

Summary Introduction

To determine: Whether gel filtration or SDS-PAGE would be accurate to find molecular mass of proteins.

Concept introduction: Gel filtration is a technique used for the separation of molecules based on the molecular size. In these techniques, molecules move through the porous of beads, diffusing into the beads with greater or lesser degrees of interaction. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analyzes the protein mixture based on size. Proteins that have higher and lower molecular mass run slowly and fast in the gel under the effect of an electric field respectively.

Answer 9

Summary Introduction

To determine: Whether gel filtration or SDS-PAGE would be accurate to find molecular mass of proteins.

Concept introduction: Gel filtration is a technique used for the separation of molecules based on the molecular size. In these techniques, molecules move through the porous of beads, diffusing into the beads with greater or lesser degrees of interaction. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analyzes the protein mixture based on size. Proteins that have higher and lower molecular mass run slowly and fast in the gel under the effect of an electric field respectively.

Answer 10

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Answer 11

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Answer 12

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Answer 13

Ch. 5 - Prob. 1E Ch. 5 - Prob. 2E Ch. 5 - 3. Which peptide has greater absorbance at 280...Ch. 5 - 4. Protein X has an absorptivity of 0.4 mL · mg?1...Ch. 5 - 5. You are using ammonium sulfate to purify...Ch. 5 - Prob. 6E Ch. 5 - 7. (a) In what order would the amino acids Arg,...Ch. 5 - Prob. 8E Ch. 5 - 9. Explain why a certain protein has an apparent...Ch. 5 - 10. Determine the subunit composition of a protein...

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