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Plasma desorption mass spectrometry coupled with conventional peptide sequencing techniques
Author(s) -
Craig A. Grey,
Engström Åke,
Bennich Hans,
Kamensky Ivan
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.1200141118
Subject(s) - mass spectrometry , peptide , chemistry , desorption , chromatography , protein mass spectrometry , peptide sequence , amino acid , biochemistry , tandem mass spectrometry , organic chemistry , adsorption , gene
The mass of intact and enzymatically derived fragments of cecropin B, an antibacterial protein from the Chinese oak silk moth, Antherea pernyi , have been determined by 252 Cf plasma desorption time‐of‐flight mass spectrometry. As a result, the carboxy terminal amino acid sequence of the protein was established.
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