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Peptide amino acid sequence analysis using matrix-assisted laser desorption/ionization and fourier transform mass spectrometry

✍ Scribed by John A. Castoro; Charles L. Wilkins; Amina S. Woods; Robert J. Cotter

Publisher
John Wiley and Sons
Year
1995
Tongue
English
Weight
455 KB
Volume
30
Category
Article
ISSN
1076-5174

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✦ Synopsis

Abstract

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 acids peptides were detected with resolving power of 8000–17 900 and mass measurement accuracy between 8 and 81 ppm for the all ^12^C 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.

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