STUDIES ON POLYMERIC STRUCTURE OF HEMOGLOBIN AND ITS RELATION TO THE FUNCTION.

A procedure was developed for obtaining the deltaA2 subunit in a physiologically active state. The isolated subunit was identified by starch gel electrophresis and tryptic peptide mapping. The number of the reactive SH group was estimated as two per chain. The oxygen equilibrium was characterized by an increased affinity toward oxygen, and absence of heme-heme interaction and the Bohr effect. The oxygen affinity was found to be lower than that of the betaA subunits. All these findings are essentially the same as those for other single subunit hemoglobins. Oxygenation properties of partially oxidized hemoglobin were examined. An increase in the oxygen affinity and a decrease in the heme-heme interaction were associated with the partial oxidation of hemoglobin Darling-Roughton effect. Quantitative relationships between the former two changes and the latter were established. The oxidation, however, had no influence upon the normal Bohr effect. Author