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Structural analysis of protein variants by mass spectrometry: characterization of haemoglobin providence using a grand-scale mass spectrometer.

作者信息

Wada Y, Fujita T, Hayashi A, Sakurai T, Matsuo T

机构信息

Osaka Medical Centre, Japan.

出版信息

Biomed Environ Mass Spectrom. 1989 Aug;18(8):563-5. doi: 10.1002/bms.1200180809.

DOI:10.1002/bms.1200180809
PMID:2804442
Abstract

A grand-scale mass spectrometer with high mass resolution and high transmission was employed for the analysis of haemoglobin variant. Two variants were isolated from a haemolysate by chromatography. Secondary ion mass spectrometry of complex peptide mixtures derived from these variants precisely determined the molecular weight of abnormal peptides. The molecular weight, 2857.4 and 2858.4, indicated the amino acid substitutions of asparagine and aspartic acid, respectively, for lysine at position 82 of beta globin chain. The mutations had been reported in haemoglobin Providence.

摘要

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