Premium
ANGIOTENSIN CONVERTING ENZYME IN THE RAT HEART: STUDIES OF ITS INHIBITION IN VITRO AND EX VIVO
Author(s) -
Fabris Bruno,
Jackson Bruce,
Cubela Rose,
Mendelsohn Frederick A. O.,
Johnston Colin I.
Publication year - 1989
Publication title -
clinical and experimental pharmacology and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.752
H-Index - 103
eISSN - 1440-1681
pISSN - 0305-1870
DOI - 10.1111/j.1440-1681.1989.tb01563.x
Subject(s) - quinapril , in vivo , ex vivo , angiotensin converting enzyme , potency , ventricle , chemistry , ace inhibitor , medicine , endocrinology , lung , pharmacokinetics , angiotensin ii , enzyme inhibitor , pharmacology , in vitro , biology , receptor , biochemistry , blood pressure , microbiology and biotechnology
SUMMARY 1. The pharmacokinetics of angiotensin converting enzyme (ACE) inhibition in rat heart and lung was evaluated in vitro and ex vivo. 2 Radioinhibitor [ 125 I]‐351A binding displacement was used to assess the relative potency of six ACE‐inhibitors (CI906, CGS14831, S9780, 351A, MK521, SQ27519) in rat heart and lung homogenates, and estimate equilibrium association constant (K a ). 3. Following oral administration of 0.3 mg/kg of Quinapril (CI928) specific binding of [ 125 I]‐351A to ACE was measured in rat heart. 4. K a for binding to ACE of each inhibitor was significantly higher in right and left atrium than in lung ( P < 0.05) or the right and left ventricle ( P < 0.005). These differences did not affect the degree or time course of inhibition in vivo in the rat myocardial ACE following Quinapril treatment. 5. Rank order of potency of the ACE inhibitors tested was CI906 = CGS14831>S9780>351A>MK521>SQ27519