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

relative content of positively and negatively charged residue
relative content of positively charged residue only
relative content of negatively charged residue only
size

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Gel Electrophoresis
In an SDS-PAGE

smaller proteins migrate more rapidly through the gel
proteins have the same charge-to-mass ratio
All of these
proteins are denatured by the SDS

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

both proteins migrate to the anode
both proteins migrate to the cathode
histones migrate to the cathode and myoglobin migrates to the anode
histones migrate to the anode and myoglobin migrates to the cathode

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Gel Electrophoresis
In SDS-PAGE, the protein sample is first

treated with a reducing agent and then with anionic detergent followed by fractionation by electrophoresis
treated with a oxidizing agent and then with anionic detergent followed by fractionation by electrophoresis
None of these
fractionated by electrophoresis then treated with an oxidizing agent followed by anionic detergent.

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