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Question: During gel filtration chromatography under native cconditions, a protein of interest elutes with a molecular weight between 500 and 550 kDA. During SDS-PAGE without 2-mercaptoethanol, the same protein migrates as a single band of approximately 13o kDA. When SDS-PAGE is carried out in the presence of 2-mercaptoethanol, the protein migrates as two bands of approximately 95 and 35 kDa. Based upon these results, describe the subunit composition of the native protein and the basis for your conclusions.

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Category:- Biology
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