Characterization of Cholecystokinin from the Human Brain

Laurence J. Miller, Ian Jardine, Edward Weissman, Vay Liang W. Go, David Speicher

Research output: Contribution to journalArticlepeer-review

39 Scopus citations


Abstract: 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(SO3)‐Met‐Gly‐Trp‐Met‐Asp‐Phe(NH2). 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.

Original languageEnglish (US)
Pages (from-to)835-840
Number of pages6
JournalJournal of neurochemistry
Issue number3
StatePublished - Sep 1984


  • Cholecystokinin
  • FAB mass spectrometry
  • Human brain peptides
  • Peptide sequencing

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience


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