[3H]Captopril binding to membrane associated angiotensin converting enzyme

Stephen M. Strittmatter, Michael S. Kapiloff, Solomon H. Snyder

Research output: Contribution to journalArticle

40 Scopus citations

Abstract

[3H]Captopril binding to membrane fractions of rat tissues is saturable and reversible with a KD of 2.4nM. [3H]Captopril binding and angiotensin converting enzyme measured with hippuryl-L-histidine-L-leucine are distributed in parallel between different tissues and brain regions, with highest levels in the choroid plexus, lung and corpus striatum. Captopril, N-(1(S)-carboxy-3-phenyl-propyl)-L-alanyl-L-proline, N-(1(S)-carboxy-3-phenyl-propyl)-L-lysyl-L-proline, teprotide, thiorphan and S-acetylcaptopril each have similar potencies for inhibition of [3H]captopril binding and of angiotensin converting enzyme. These data strongly indicate that [3H]Captopril binding evaluation should help clarify the localization and function of angiotensin converting enzyme and assist in defining pharmacologic actions of captopril.

Original languageEnglish (US)
Pages (from-to)1027-1033
Number of pages7
JournalBiochemical and biophysical research communications
Volume112
Issue number3
DOIs
StatePublished - May 16 1983

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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