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Characterization of Cholecystokinin from the Human Brain
Author(s) -
Miller Laurence J.,
Jardine Ian,
Weissman Edward,
Go Vay Liang W.,
Speicher David
Publication year - 1984
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1984.tb12806.x
Subject(s) - cholecystokinin , peptide , chemistry , biochemistry , peptide sequence , human brain , amino acid , fast atom bombardment , molecular mass , size exclusion chromatography , chromatography , mass spectrometry , biology , gene , receptor , enzyme , neuroscience
Human forms of cholecystokinin have not previously been characterized chemically. In this study, we have extracted and purified the predominant molecular form of cholecystokinin present in human cerebral cortex. The peptide was characterized by amino acid analysis, automated peptide sequencing, and fast atom bombardment mass spectrometry. It appears to be identical to porcine cholecystokinin‐octapeptide, with the sequence of Asp‐Tyr(SO 3 )‐Met‐Gly‐Trp‐Met‐Asp‐Phe(NH 2 ). This structural identity is consistent with the observations that the peptide in human brain and porcine cholecystokinin‐octapeptide are recognized similarly by a battery of antisera to porcine cholecystokinin; that they coelute from several chromatographic systems, including gel filtration, ion exchange, and reversed‐phase; and that they possess similar biological activities.