Variation in angiotensin-converting enzyme (ACE) inhibitor affinity at two binding sites on rat pulmonary ACE: influence on bradykinin hydrolysis.

doi:10.1111/j.1440-1681.1992.tb00470.x

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Article

Variation in angiotensin-converting enzyme (ACE) inhibitor affinity at two binding sites on rat pulmonary ACE: influence on bradykinin hydrolysis.

Clinical and experimental pharmacology & physiology - 1 May 1992

Perich R B, Jackson B, Johnston C I

Abstract excerpt

1. ACE from rat lung and testis was characterized by radioligand binding studies using [125I]-Ro 31-8472, the radioiodinated hydroxy derivative of the potent ACE inhibitor cilazaprilat. 2. Analysis of the displacement of [125I]-Ro 31-8472 from ACE by ACE inhibitors of different structure by the L...

Topics

Angiotensin-Converting Enzyme Inhibitors
Animals
Binding Sites
Bradykinin
Genetic Variation
Hydrolysis
Iodine Radioisotopes
Kinetics
Lung
Male
Peptidyl-Dipeptidase A
Pyridazines
Radioligand Assay
Rats
Rats, Inbred Strains
Structure-Activity Relationship
Testis

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PMID: 1325885
DOI: 10.1111/j.1440-1681.1992.tb00470.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1325885-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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