Gel Electrophoresis

In isoelectric focusing, proteins are separated on the basis of their

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Question: In isoelectric focusing, proteins are separated on the basis of their
[A].

relative content of positively charged residue only

[B].

relative content of negatively charged residue only

[C].

size

[D].

relative content of positively and negatively charged residue

Answer: Option D

Explanation:

No answer description available for this question.

In SDS-PAGE, the protein sample is first

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Question: In SDS-PAGE, the protein sample is first
[A].

treated with a reducing agent and then with anionic detergent followed by fractionation by electrophoresis

[B].

fractionated by electrophoresis then treated with an oxidizing agent followed by anionic detergent.

[C].

treated with a oxidizing agent and then with anionic detergent followed by fractionation by electrophoresis

[D].

none of the above

Answer: Option A

Explanation:

No answer description available for this question.

In an SDS-PAGE

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Question: In an SDS-PAGE
[A].

proteins are denatured by the SDS

[B].

proteins have the same charge-to-mass ratio

[C].

smaller proteins migrate more rapidly through the gel

[D].

all of the above

Answer: Option D

Explanation:

No answer description available for this question.

Electrophoresis of histones and myoglobin under non-denaturing conditions (pH = 7.0) results in

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Question: Electrophoresis of histones and myoglobin under non-denaturing conditions (pH = 7.0) results in
[A].

both proteins migrate to the anode

[B].

histones migrate to the anode and myoglobin migrates to the cathode

[C].

histones migrate to the cathode and myoglobin migrates to the anode

[D].

both proteins migrate to the cathode

Answer: Option C

Explanation:

No answer description available for this question.