Ferritin is treated with SDS or SDS and b-mercaptoethanol and subjected to polyacrylamide gel electrophoresis. Only when very large amounts of bisacrylamide are added do you see two separate bands on the gel at relative migrations of 4.0245 and 3.9375 and the results are the same with and without b-mercaptoethanol. You decide to call these the light and heavy chains of ferritin.
What are the actual sizes of the light and heavy chains of ferritin based on the SDS-PAGE data? What types of interactions hold these proteins together in the structure of ferritin?
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