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Fast atom bombardment/tandem mass spectrometry of physalaemin‐like peptides
Author(s) -
Harvan D. J.,
Hass J. R.,
Wilson W. E.,
Hamm C.,
Boyd R. K.,
Yajima H.,
Klapper D. G.
Publication year - 1987
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.1200140607
Subject(s) - fast atom bombardment , protonation , chemistry , peptide , tandem mass spectrometry , mass spectrometry , residue (chemistry) , mass spectrum , ion , stereochemistry , amino acid , chromatography , organic chemistry , biochemistry
Fragment ion spectra obtained from collision‐induced decomposition of protonated molecular ions have been used to determine amino acid sequences of several physalaemin‐like peptides which were recently purified from rabbit stomach. This technique was chosen because the peptides were available in microgram quantities and were anticipated to contain pyroglutamate as the blocked N‐terminal residue. Such spectra of several synthetic analogs of the naturally occurring peptides were obtained and analyzed to confirm the veracity of this peptide sequencing strategy. In addition, methyl ester derivatives of these synthetic peptides provided a crucial test for the spectral interpretation via the mass shifts thus induced.