Association of Radioactive Chromium with Various Components of Hemoglobin

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Abstract
1) When normal hemoglobin was labeled with Cr51 by incubation of whole blood with Na2Cr51O4, or by incubation of hemolysates with either Na2Cr51O4 or Cr51Cl3, most of the Cr51 activity was associated with the electrophoretically rapid hemoglobin A3. The formation of a Cr51 hemoglobin complex with an isoelectric point lower than that of hemoglobin was thought to be the most likely explanation of this finding.4 2) The radioactivity of Cr51-labeled hemolysates containing hemoglobin S, C, and A was found to be associated with the more rapid electrophoretic components. This finding supports the hypothesis of a lower isoelectric point of a Cr-hemoglobin complex. 3) The association of Cr51 activity with the polypeptide chains of hemoglobin was studied by two approaches: 1) determination of the labeling of components in hemolysates containing hemoglobin A (αA2 βA2) and hemoglobin H (βA4), and 2) determination of the labeling of polypeptide chains of Cr51-labeled normal hemoglobin separated by the method of Huehns and co-workers.12 Cr51 activity was found in both the naturally occurring β chain component (hemoglobin H) and in the β chain component prepared by the method of Huehns and co-workers.12 These findings support the hypothesis of others5,6 that β chains of hemoglobin have a greater affinity for chromium than do α chains.