Abstract
The equilibria between oxygen and four different kinds of abnormal hemoglobin, Hb-DPunjb, Hb-D with another unknown abnormality in the β-chain, Hb-S and Hb-Lepore have been determined. Total red blood cell hemolysates as well as isolated components (DEAE-cellulose chromatography) were studied.The two Hb-D abnormalities in isolated forms showed a slight but distinct increase in oxygen affinities, while their Bohr effects were not altered. Red blood cell hemolysates of sickle-cell anemia patients failed to show a significant change in the affinity for oxygen. The similarity of the oxygen equilibria of Hb-S and Hb-A containing hemolysates was demonstrated with the use of potassium phosphate buffer of varying molarities.A marked increase in oxygen affinity of pure Hb-Lepore as compared to normal Hb-A was found. The equilibrium between oxygen and this Hb-type was comparable with those found for Hb-A2 and its variant Hb-A2′. No change in the Bohr effect was note. A small but distinct increase in the oxygen affinity of a red blood cell hemolysates of a Hb-Lepore trait carrier was also demonstrable.
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