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Enzymatic cleavage directly on the probe tip for mass spectrometric identification of peptides
Author(s) -
HafokPeters Ch.,
MaurerFogy I.,
Schmid E. R.
Publication year - 1990
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.1200190311
Subject(s) - mass spectrometry , chemistry , fast atom bombardment , cleavage (geology) , peptide , enzyme , molecular mass , chromatography , amino acid , peptide sequence , amino acid residue , analytical chemistry (journal) , biochemistry , materials science , fracture (geology) , composite material , gene
Fast atom bombardment mass spectrometry was used in direct combination with enzymatic cleavages by endopeptidases for the identification of peptides derived from recombinant proteins. By this fast and simple reaction on the probe tip, the enzymes produced a mixture of smaller peptides. Molecular weights were calculated in advance and used for verification of the amino acid sequence of the original peptide as well as for partial structure determinations. Since the enzymatic reaction took place directly on the probe tip, sample material and time was saved. This technique may be applied especially in such cases where mass spectrometry alone does not give sufficient information and if the mass range of the instrument is limited, e.g. to 2000 daltons.