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Secondary ion mass spectra of tryptic peptides of human hemoglobin chains
Author(s) -
Katakuse I.,
Ichihara T.,
Nakabushi H.,
Matsuo T.,
Matsuda H.,
Wada Y.,
Hayashi A.
Publication year - 1984
Publication title -
biomedical mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 0306-042X
DOI - 10.1002/bms.1200110804
Subject(s) - chemistry , protonation , mass spectrum , ion , globin , hemoglobin , molecular mass , mass spectrometry , chromatography , biochemistry , organic chemistry , enzyme
Secondary ion mass spectra of tryptic peprides of human globin α‐, β‐, γ and α‐chains were studied. Almost all mass peaks of protonated molecular ions of tryptic peptides were observed and they were very stable and abundant. The present results show the possibilities for quantitative analysis of two γ‐globin species: A γ and G γ chains, and for structural analysis of unknown abnormal hemoglobins.