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Peptide sequencing by partial acid hydrolysis and high resolution plasma desorption mass spectrometry
Author(s) -
Zubarev R. A.,
Chivanov V. D.,
Håkansson P.,
Sundqvist B. U. R.,
Ens Werner
Publication year - 1994
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1290081109
Subject(s) - chemistry , peptide , mass spectrometry , edman degradation , hydrolysis , chromatography , acid hydrolysis , peptide sequence , organic chemistry , biochemistry , gene
A method of deriving peptide sequence information using partial acid hydrolysis in combination with accurate mass measurements and immonium ion analysis provided by high‐resolution plasma desorption mass spectrometry has been developed. The technique is very simple in terms of the chemistry and involves a short‐time (3–30 min) incubation of the peptide in 1N–6N HCl at 100–110°C with subsequent mass spectrometric analysis. Partial acid hydrolysis is found to produce sequence‐specific segments, often ladder‐like, although not always a complete set. Two application examples of the method are given: the linear peptide bradykinin and desmopressin, a peptide with an internal SS bond and a non‐amino‐acid constituent. The technique has proved to be particularly useful in cases where some a priori information on the peptide structure was already known or where the automated Edman degradation technique might yield erratic results or not work at all.