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Linked scan investigation of peptide degradation initiated by liquid secondary ion mass spectrometry
Author(s) -
Renner D.,
Spiteller G.
Publication year - 1988
Publication title -
biomedical and environmental mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 0887-6134
DOI - 10.1002/bms.1200150204
Subject(s) - zwitterion , chemistry , peptide , mass spectrometry , ion , carboxylate , imine , degradation (telecommunications) , tandem mass spectrometry , amino acid , chromatography , stereochemistry , organic chemistry , biochemistry , molecule , telecommunications , computer science , catalysis
[MH] + ions of peptides are degraded in one step to acyl ions, indicating the presence of different [MH] + species. In contrast to protons, cations are added mainly at the carboxylate function of a peptide zwitterion. These species are degraded by loss of the C ‐terminal amino acid in the form of CO and an imine.