Linked scan investigation of peptide degradation initiated by liquid secondary ion mass spectrometry | Zendy

Renner D. | Zendy; Spiteller G. | Zendy

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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.

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