Is the C-terminal flanking peptide of rat cholecystokinin double sulphated?

T. E. Adrian, J. Domin, A. J. Bacarese-Hamilton, S. R. Bloom

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

Abstract

A specific radioimmunoassay was developed to the predicted nine amino acid C-terminal flanking peptide of cholecystokinin (peptide serine serine, PSS). In aqueous extracts of rat brain, PSS was undetectable unless the extracts were first treated with arylsulphatase, which also resulted in desulphation of cholecystokinin. The reverse-phase HPLC analysis of partially desulphated extracts showed the presence of two peaks intermediate to the naturally occurring and the completely desulphated forms. It is therefore proposed that the CCK-flanking peptide PSS has both tyrosine residues sulphated.

Original languageEnglish
Pages (from-to)5-8
Number of pages4
JournalFEBS Letters
Volume196
Issue number1
DOIs
Publication statusPublished - Feb 3 1986
Externally publishedYes

Keywords

  • (Rat brain)
  • Cholecystokinin
  • Desulfation
  • Flanking peptide
  • HPLC
  • Radioimmunoassay

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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