Hemoglobin Hirose: α2β237(C3) Tryptophan Yielding Serine

Author:

YAMAOKA KOTARO1

Affiliation:

1. First Department of Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan.

Abstract

Abstract During an electrophoretic screening survey for hemoglobinopathies in western Japan, a slow-moving variant of hemoglobin A, to be designated hemoglobin Hirose, was found in a family of Japanese origin. Chemical characterization of hemoglobin Hirose revealed that tryptophan at the 37th position of the β-chain was replaced by serine, the third residue of C-helix of the β-chain involving contacts between αl and β2 subunits. Even though the oxygen equilibrium of this hemoglobin was abnormal, none of the family members showed any clinically significant symptoms.

Publisher

American Society of Hematology

Subject

Cell Biology,Hematology,Immunology,Biochemistry

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