Characterization of a new fetal hemoglobin variant, Hb F Izumi A gamma 6Glu replaced by Gly, by molecular secondary ion mass spectrometry.

作者: Yoshinao Wada , Akira Hayashi , Fusimura Masanori , Itsuo Katakuse , Toshio Ichihara

DOI: 10.1016/0167-4838(83)90231-5

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摘要: Abstract Molecular secondary ion mass spectrometry has characterized the structure of a new fetal hemoglobin variant, Hb F Izumi, without separation peptides or amino acid analysis. First, spectrum tryptic digest abnormal γ globin revealed decreased by 72 units in molecular peptide T-1,2, indicating presence Glu Gly substitution. Next, analysis produced addition staphylococcal protease, which specifically cleaves glutamyl bonds, determined site substitution at 6th glutamic residue T-1,2 contains two residues. Since this spectrometric approach provides digitalized data on analysis, we call it ‘digit printing’. The high sensitivity technique is especially promising for abnormality various genetic disorders.

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