Gel Electrophoresis
Proteins are separated in an SDS-PAGE experiment on the basis of their

different isoelectric points
negatively charged side chains
molecular weight
positively charged side chains

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Gel Electrophoresis
In an SDS-PAGE

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

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

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

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

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