Open AccessC‐terminal sequencing of protein
Author(s) -
TSUGITA Akira,
TAKAMOTO Keiji,
KAMO Masaharu,
IWADATE Hiromoto
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb16975.x
Subject(s) - chemistry , oxazolone , hydrolysis , residue (chemistry) , fast atom bombardment , mass spectrometry , aspartic acid , serine , electrospray ionization , peptide bond , chromatography , peptide , amino acid , acid hydrolysis , organic chemistry , biochemistry , enzyme
Peptides or proteins were hydrolyzed by vapors of 90% pentafluoropropionic acid or heptafluorobutyric acid at 90°C for various time periods. The hydrolyzate mixtures analyzed by both fast‐atom‐bombardment and electrospray ionization mass spectrometry showed a series of C‐terminal successive degradation molecular ions. The degradation reaction may be due to the selective formation of an oxazolone ring at the C‐terminal amino acid, followed by hydrolytic removal of the C‐terminal amino acid. The major side reactions were cleavages of the peptide bonds at the C side of the internal aspartic acid residue and the N side of serine residue.