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- W2020953831 abstract "The primary structure of a new variant of human adult hemoglobin, Hb MOsaka, was studied. The peptide chain anomaly was determined by hybridization with canine hemoglobin and by amino acid analysis of two chains separated by counter-current distribution. Tryptic digests of the abnormal chain were separated by column chromatography, followed by paper chromatography. The amino acid composition of digests from Hb A and Hb MOsaka are remarkably alike with the exception of one peptide, αTpVII, which contains residues from 57 to 60 of the α-chain. Consequently it was found that in Hb MOsaka a tyrosine residue replaces the histidine residue which is present in position 58 in the α-chain of Hb A. The differences between the absorption spectra of Hb A and Hb MOsaka were also studied and it has been noticed that the pattern of the absorption spectrum of Hb MOsaka was identical with that of Hb MBoston." @default.
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- W2020953831 date "1965-03-01" @default.
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- W2020953831 title "The structural study on a new hemoglobin variant, Hb MOsaka" @default.
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- W2020953831 doi "https://doi.org/10.1016/0304-4165(65)90159-5" @default.
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