A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography. When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol, three bands are again formed, this time with molecular masses of 160, 90, and 60 kDa. Determine the subunit composition of the protein and clearly explain how you came to this determination.

Biochemistry
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Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
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Chapter1: Biochemistry: An Evolving Science
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A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography.
When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives
three bands with molecular masses of 180, 160, and 60 kDa. When electrophoresis is carried out in the
presence of SDS and dithiothreitol, three bands are again formed, this time with molecular masses of
160, 90, and 60 kDa. Determine the subunit composition of the protein and clearly explain how you
came to this determination.
Transcribed Image Text:A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography. When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol, three bands are again formed, this time with molecular masses of 160, 90, and 60 kDa. Determine the subunit composition of the protein and clearly explain how you came to this determination.
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