PEPTIDE AMINO-ACID-SEQUENCE ANALYSIS USING MATRIX-ASSISTED LASER-DESORPTION IONIZATION AND FOURIER-TRANSFORM MASS-SPECTROMETRY

被引：29

作者：

CASTORO, JA ^{[1
]}

WILKINS, CL ^{[1
]}

WOODS, AS ^{[1
]}

COTTER, RJ ^{[1
]}

机构：

[1] JOHNS HOPKINS UNIV,SCH MED,DEPT PHARMACOL & MOLEC SCI,MIDDLE ATLANTIC MASS SPECTROMETRY LAB,BALTIMORE,MD 21205

来源：

JOURNAL OF MASS SPECTROMETRY | 1995年 / 30卷 / 01期

关键词：

D O I：

10.1002/jms.1190300115

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

High-performance matrix-assisted laser desorption/ionization (MALDI) using 7 T Fourier transform mass spectrometry (FTMS) was investigated for peptide amino acid sequence analysis. Two synthetic peptides representative of the type which would be displayed by major histocompatibility complex molecules from tumor cells were investigated by MALDI/FTMS. Molecular ions of the two 9-amino acid peptides were detected with resolving power of 8000-17900 and mass measurement accuracy between 8 and 81 ppm for the all C-12 isotope ions. An ultra-high resolution spectrum (RP 300 000) for the molecular ion of one of the two peptides was obtained. Structurally useful sequence information was obtained by use of surface-induced dissociation (SID) of the molecular ion species. Interestingly, SID of a sodium-attached peptide molecular ion resulted in the production of numerous sodium-attached sequence ions.

引用

页码：94 / 98

页数：5

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