Some Properties of Hemoglobin Gun Hill

Jayalakshmi Murari Laboratory of Protein Chemistry and Comprehensive Sickle Cell Center, HCC, Augusta, Ga, 30902

L. L. Smith Dept. of Cell and Molecular Biology, MCG, Augusta, Ga, 30902

J. B. Wilson Laboratory of Protein Chemistry and Comprehensive Sickle Cell Center, HCC, Augusta, Ga, 30902

R. G. Schneider Dept. of Pediatrics, University of Texas, Medical Branch, Galveston, Texas, 77550

T. H. J. Huisman Laboratory of Protein Chemistry and Comprehensive Sickle Cell Center, HCC, Augusta, Ga, 30902; Dept. of Cell and Molecular Biology, MCG, Augusta, Ga, 30902

Abstract

Hb Gun Hill has been found in an asymptomatic black female living in Alabama; neither her parents nor her two siblings carry the variant. The deletion of five mino acid residues in the β chain of lib Gun Hill (α₂β₂ 91-95 deleted) causes this vartant to have a high oxygen affinity, an interaction coefficient of unity and an absence of the Bohr effect. The rate of oxidation of liganded Hb Gun Hill by the ferricyanide ion follovs first-order kinetics. Hb Gun Hill is to a great extent dissociated into dimers over a wide range of pH values.

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Some Properties of Hemoglobin Gun Hill

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Some Properties of Hemoglobin Gun Hill

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