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Rapid analysis of a peptide by fast‐atom bombardment mass spectrometry after polyacrylamide gel electrophoresis
Author(s) -
Camilleri P.,
Haskins N. J.,
Hill A. J.
Publication year - 1989
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.1290031008
Subject(s) - chemistry , chromatography , fast atom bombardment , mass spectrometry , polyacrylamide gel electrophoresis , peptide , protonation , acetic acid , polyacrylamide , gel electrophoresis , electrophoresis , capillary electrophoresis , analytical chemistry (journal) , ion , biochemistry , organic chemistry , polymer chemistry , enzyme
Gel electrophoresis has been a powerful technique for the separation of peptides and proteins for many years. After electrophoresis separation on a polyacrylamide gel, the peptide bradykinin was localized using Coomassie Blue as a staining dye. Excess dye was removed by washing the gel with water, For mass spectrometric analysis, bands containing the peptide were crushed, extracted with acetic acid and the eluent applied to the fast‐atom bombardment probe. Under these conditions the protonated molecule of bradykinin was clearly observed. Also apparent were sequence ions at about the same intensity observed from authentic bradykinin.