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Biochemistry - Gel Electrophoresis

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Exercise : Gel Electrophoresis - Section 1
  • Gel Electrophoresis - Section 1
1.
In an SDS-PAGE
proteins are denatured by the SDS
proteins have the same charge-to-mass ratio
smaller proteins migrate more rapidly through the gel
all of the above
Answer: Option
Explanation:
No answer description is available. Let's discuss.
2.
Proteins can be visualized directly in gels by
staining them with the dye
using electron microscope only
measuring their molecular weight
none of these
Answer: Option
Explanation:
No answer description is available. Let's discuss.
3.
In SDS-PAGE, the protein sample is first
treated with a reducing agent and then with anionic detergent followed by fractionation by electrophoresis
fractionated by electrophoresis then treated with an oxidizing agent followed by anionic detergent.
treated with a oxidizing agent and then with anionic detergent followed by fractionation by electrophoresis
none of the above
Answer: Option
Explanation:
No answer description is available. Let's discuss.
4.
Electrophoresis of histones and myoglobin under non-denaturing conditions (pH = 7.0) results in
both proteins migrate to the anode
histones migrate to the anode and myoglobin migrates to the cathode
histones migrate to the cathode and myoglobin migrates to the anode
both proteins migrate to the cathode
Answer: Option
Explanation:
No answer description is available. Let's discuss.
5.
In isoelectric focusing, proteins are separated on the basis of their
relative content of positively charged residue only
relative content of negatively charged residue only
size
relative content of positively and negatively charged residue
Answer: Option
Explanation:
No answer description is available. Let's discuss.
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