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Matrix-assisted laser desorption/ionization time-of-flight mass spectrometric observation of a peptide triplet induced by thermal cleavage of cystine
Cited 26 time in
Web of Science
Cited 22 time in Scopus
- Authors
- Issue Date
- 2001
- Publisher
- John Wiley & Sons Inc.
- Citation
- Rapid Communications in Mass Spectrometry, Vol.15 No.23, pp.2296-2300
- Abstract
- Heat-induced (90 degreesC, 30 min) beta -elimination of a cystine residue leads to cleavage of a disulfide bond and produces a set of three peptides with a cysteine residue, a thiocysteine residue (+32Da), and a dehydroalanine residue (-34Da). This characteristic feature was observed from somatostatin and insulin by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Mass spectrometric observation of this triplet is useful in identifying the presence of a cystine residue in a peptide, and could assist mass spectrometric identification of the peptide from a database. Copyright (C) 2001 John Wiley & Sons, Ltd.
- ISSN
- 0951-4198
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