Biochemistry
Biochemistry
6th Edition
ISBN: 9781337359573
Author: Reginald H. Garrett; Charles M. Grisham
Publisher: Cengage Learning US
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Chapter 15, Problem 16P
Interpretation Introduction

To illustrate:

The two monomer conformations, tetramer and trimer showing how tetramer is stable.

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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 (DTT), three bands again form, this time with molecular masses of 160, 90, and 60 kDa. How many subunits does the protein have, and what is the molecular mass of each? four subunits: 180, 160, 90, and 60 kDa three subunits: 180, 160, and 60 kDa three subunits: 160, 90, and 60 kDa four subunits: 160, 90, 90, and 60 kDa Correct Answer
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