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• W2023531661 startingPage "244" @default.
• W2023531661 abstract "Molecular secondary ion mass spectrometry has characterized the structure of a new fetal hemoglobin variant, Hb F Izumi, without separation of peptides or amino acid analysis. First, the mass spectrum of a tryptic digest of the abnormal γ globin revealed a decreased by 72 mass units in the molecular mass of peptide T-1,2, indicating the presence of a Glu å Gly substitution. Next, the analysis of the digest produced by the addition of staphylococcal protease, which specifically cleaves glutamyl peptide bonds, determined the site of substitution at 6th glutamic acid residue in peptide T-1,2 which contains two glutamic acid residues. Since this mass spectrometric approach provides digitalized data on peptide analysis, we call it ‘digit printing’. The high sensitivity of this technique is especially promising for the analysis of molecular abnormality in various genetic disorders." @default.
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• W2023531661 date "1983-12-01" @default.
• W2023531661 modified "2023-09-26" @default.
• W2023531661 title "Characterization of a new fetal hemoglobin variant, Hb F Izumi γ, by molecular secondary ion mass spectrometry" @default.
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• W2023531661 doi "https://doi.org/10.1016/0167-4838(83)90231-5" @default.
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