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.

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