β-Endorphin inhibits met-enkephalin breakdown by a brain aminopeptidase: Structure-activity relationships

Koon Sea Hui, László Gráf, Abel Lajtha

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

An aminopeptidase solubilized and isolated from rat brain membranes selectively splits the Tyr1-Gly2 peptide bond of Met-enkephalin. βh-Endorphin, which is apparently resistant to the aminopeptidase, inhibited the action of this peptidase on Met-enkephalin degradation competitively; the Ki value was 11.5 μM. Arg0h-endorphin was found to be 10 times more potent than βh-endorphin. From further structure-activity data it is concluded that the N-terminal amino group and some residues within region 18-31 of the β-endorphin structure are cooperatively involved in binding to the active site of the aminopeptidase.

Original languageEnglish
Pages (from-to)1482-1487
Number of pages6
JournalBiochemical and biophysical research communications
Volume105
Issue number4
DOIs
Publication statusPublished - Apr 29 1982

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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