Abstract
The oxygen binding property and molecular stability of Hb C-Harlem (Hb CH) (β6 Glu+Val, β73 Asp+Asn) were studied in comparison with those of Hb A and Hb S. The oxygen affinity and Bohr effect of purified Hb CH with and without organic phosphates were similar to those of purified Hb A and Hb S. The oxygen affinities of red cell suspensions obtained from the patient with Hb S-CH were lower than those of Hb S and Hb A. The level of 2,3-DPG was elevated by more than 50% of the normal level. The stability of various liganded forms of Hb CH was determined by mechanical shaking and heat denaturation. The oxy-, carbonmonoxy-, and met-forms of Hb CH were 2–3 times less stable than corresponding forms of Hb S during mechanical shaking. The results of the shaking experiments on deoxy-Hb CH differed drastically from those obtained on deoxy-Hb S, with deoxy-Hb CH being 17 times less stable than deoxy-Hb S. The rate of precipitation of the various ligands of Hb CH was pH dependent, with the rate being faster in an alk...
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