Methionine enkephalin is hydrolyzed by aminopeptidase N on CD4+ and CD8+ spleen T cells

B. C. Miller, Dwain L Thiele, L. B. Hersh, G. L. Cottam

Research output: Contribution to journalArticle

24 Scopus citations

Abstract

Exogenous methionine enkephalin incubated with CD4+ or CD8+ T cells purified from murine spleen is metabolized primarily, if not exclusively, by aminopeptidase N (aminopeptidase M, EC 3.4.11.2), a membrane-anchored ectopeptidase. The enzyme activity is identified by its substrate specificity, sensitivity to inhibition by amastatin, and immunoreactivity with antibody to rat kidney aminopeptidase N. Activation of CD4+ T cells results in a small increase per cell in aminopeptidase N activity.

Original languageEnglish (US)
Pages (from-to)174-179
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume311
Issue number1
DOIs
StatePublished - May 1994

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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