HB F-Meinohama or α₂γ₂ (5 GLU-GLY; 75 ILE; 136 GLY)

Y. Ohta Department, of Medicine Faculty of Medicine, Ehime University Ehime-Ken 791–02, Japan

S. Saito Department, of Medicine Faculty of Medicine, Ehime University Ehime-Ken 791–02, Japan

S. Fujita Department, of Medicine Faculty of Medicine, Ehime University Ehime-Ken 791–02, Japan

J. B. Wilson Department of Cell and Molecular Biology, Laboratory of Protein Chemistry and Comprehensive Sickle Cell Center, Medical College of Georgia, Augusta, GA, 30912, USA

H. Lam Department of Cell and Molecular Biology, Laboratory of Protein Chemistry and Comprehensive Sickle Cell Center, Medical College of Georgia, Augusta, GA, 30912, USA

T. H. J. Huisman Department of Cell and Molecular Biology, Laboratory of Protein Chemistry and Comprehensive Sickle Cell Center, Medical College of Georgia, Augusta, GA, 30912, USA

Abstract

During a survey of blood samples from newborn babies, a new fetal hemoglobin variant was observed which had a substitution of the normally occurring glutaminyl residue at position y5 (A2) for a glycyl residue, The abnormal y chain had an iso-leucyl residue at position 75 and a glycyl residue at position 136.

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HB F-Meinohama or α₂γ₂ (5 GLU-GLY; 75 ILE; 136 GLY)

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HB F-Meinohama or α2γ2 (5 GLU-GLY; 75 ILE; 136 GLY)

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HB F-Meinohama or α₂γ₂ (5 GLU-GLY; 75 ILE; 136 GLY)