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C‐terminal sequencing of peptides using electrospray ionization mass spectrometry
Author(s) -
Rosnack Kenneth J.,
Stroh Justin G.
Publication year - 1992
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.1290061102
Subject(s) - chemistry , electrospray ionization , amino acid , chromatography , mass spectrometry , electrospray , peptide , peptide sequence , carboxypeptidase , protein mass spectrometry , glucagon , carboxypeptidase a , biochemistry , enzyme , hormone , gene
A low‐flow reactor is described for the on‐line monitoring of peptides digested with carboxypeptidase P by electrospray ionization. Two peptides were analyzed using this technique: glucagon (average MW 3482.8 Da), and apomyoglobin (average MW 16 951.5). Both peptides gave interpretable results. The first 19 amino acids of glucagon were successfully sequenced. Apomyoglobin yielded sequence information to the 30th amino acid with some gaps. At 300 nL/min, 50% of the first 30 amino acids were sequenced and at 1μL/min, 67% of the first 30 amino acids were observed.