Abstract
The distribution of radioactive chromium on proteins isolated in the soluble fraction of the human erythrocyte was studied utilizing sodium dodecyl sulfate polyacrylamide gel electrophoresis. The radioactive label was associated with the hemoglobin monomeric subunit and, unexpectedly, with another soluble fraction protein. This protein was approximately 6% of the total isolated protein, contained approximately 20% of the radioactivity, and had an estimated molecular weight of 26,700 daltons.
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