Abstract
Adult hemoglobin was partially oxidized with ferricyanide and the oxygen equilibrium in 0.4 M-phosphate was studied. An increase in the oxygen affinity and a decrease in the heme-heme interaction were associated with the partial oxidation of hemoglobin. The results confirmed those of Darling and Roughton (1942). Quantitative relationships between partial oxidation and these functional changes were established. The oxidation had no influence upon the normal Bohr effect. It was shown that the changes in the oxygen equilibria were not caused by the increase of one positive net charge per heme oxidized, nor by ferrocyanide bound to hemoglobin, nor by the oxidation of SH groups. Based upon the present results, physiological implications of methemoglobinemia were quantitatively discussed.
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