Premium
Identification of variant forms of the neuroendocrine peptide galanin
Author(s) -
Norberg Åke,
Griffiths William J.,
Hjelmqvist Lars,
Jörnvall Hans,
Rökaeus Åke
Publication year - 2004
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.1522
Subject(s) - galanin , chemistry , peptide , tandem mass spectrometry , fragmentation (computing) , enteroendocrine cell , biochemistry , endocrine system , mass spectrometry , chromatography , neuropeptide , receptor , hormone , biology , ecology
Abstract Galanin is a neuroendocrine peptide widely distributed in the central and peripheral nervous systems and in endocrine tissues. Using radioimmunoassays, chromatographic separations, and tandem mass spectrometry, we have identified a series of five variant forms of galanin purified from porcine upper intestine. The modified variants include three β ‐aspartyl‐shifted forms, an oxidized form containing Trp monooxide, and an N‐terminally truncated form. All were found to be C‐terminally amidated. At least the β ‐aspartyl‐shifted forms could be of native occurrence. Mechanistic explanations of the mass spectrometric fragmentation patterns of the different forms are suggested. Copyright © 2004 John Wiley & Sons, Ltd.