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

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

Research output: Contribution to journalArticle

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

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Captopril
Peptidyl-Dipeptidase A
Membranes
alanylproline
Teprotide
Thiorphan
Tissue
Pharmacologic Actions
Corpus Striatum
Choroid Plexus
Histidine
Proline
Leucine
Rats
Brain
Lung

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

[3H]Captopril binding to membrane associated angiotensin converting enzyme. / Strittmatter, Stephen M.; Kapiloff, Michael S.; Snyder, Solomon H.

In: Biochemical and Biophysical Research Communications, Vol. 112, No. 3, 16.05.1983, p. 1027-1033.

Research output: Contribution to journalArticle

Strittmatter, Stephen M. ; Kapiloff, Michael S. ; Snyder, Solomon H. / [3H]Captopril binding to membrane associated angiotensin converting enzyme. In: Biochemical and Biophysical Research Communications. 1983 ; Vol. 112, No. 3. pp. 1027-1033.
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