人血红蛋白链胰蛋白酶肽段的二次离子质谱
Secondary ion mass spectra of tryptic peptides of human hemoglobin chains.
作者信息
Katakuse I, Ichihara T, Nakabushi H, Matsuo T, Matsuda H, Wada Y, Hayashi A
出版信息
Biomed Mass Spectrom. 1984 Aug;11(8):386-91. doi: 10.1002/bms.1200110804.
PMID:6478045
Abstract
Secondary ion mass spectra of tryptic peptides of human globin alpha-, beta-, gamma and delta-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 gamma-globin species: A gamma and G gamma chains, and for structural analysis of unknown abnormal hemoglobins.
摘要
对人球蛋白α链、β链、γ链和δ链的胰蛋白酶肽段的二次离子质谱进行了研究。观察到了胰蛋白酶肽段质子化分子离子的几乎所有质量峰，并且它们非常稳定且丰度高。目前的结果显示了对两种γ球蛋白种类：Aγ链和Gγ链进行定量分析以及对未知异常血红蛋白进行结构分析的可能性。
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