amastatin and ramiprilat

amastatin has been researched along with ramiprilat* in 1 studies

Other Studies

1 other study(ies) available for amastatin and ramiprilat

Article	Year
Identification of kallidin degrading enzymes in the isolated perfused rat heart. Japanese journal of pharmacology, 1999, Volume: 79, Issue:1 Kallidin (KD) is an important vasoactive kinin whose physiological effects are strongly dependent on its degradation through local kininases. In the present study, we examined the spectrum of these enzymes and their contribution to KD degradation in isolated perfused rat hearts. By inhibiting angiotensin-converting enzyme (ACE), aminopeptidase M (APM) and neutral endopeptidase (NEP) with ramiprilat (0.25 microM), amastatin (40 microM) and phosphoramidon (1 microM), respectively, relative kininase activities were obtained. APM (44%) and ACE (35%) are the main KD degrading enzymes in rat heart; NEP (7%) plays a minor role. A participation of carboxypeptidase N (CPN) could not be found. Topics: Aminopeptidases; Angiotensin-Converting Enzyme Inhibitors; Animals; Anti-Bacterial Agents; Glycopeptides; In Vitro Techniques; Kallidin; Male; Myocardium; Neprilysin; Peptide Hydrolases; Peptides; Peptidyl-Dipeptidase A; Perfusion; Protease Inhibitors; Ramipril; Rats; Rats, Wistar	1999

Article

Year

Identification of kallidin degrading enzymes in the isolated perfused rat heart.

Japanese journal of pharmacology, 1999, Volume: 79, Issue:1

Kallidin (KD) is an important vasoactive kinin whose physiological effects are strongly dependent on its degradation through local kininases. In the present study, we examined the spectrum of these enzymes and their contribution to KD degradation in isolated perfused rat hearts. By inhibiting angiotensin-converting enzyme (ACE), aminopeptidase M (APM) and neutral endopeptidase (NEP) with ramiprilat (0.25 microM), amastatin (40 microM) and phosphoramidon (1 microM), respectively, relative kininase activities were obtained. APM (44%) and ACE (35%) are the main KD degrading enzymes in rat heart; NEP (7%) plays a minor role. A participation of carboxypeptidase N (CPN) could not be found.

Topics: Aminopeptidases; Angiotensin-Converting Enzyme Inhibitors; Animals; Anti-Bacterial Agents; Glycopeptides; In Vitro Techniques; Kallidin; Male; Myocardium; Neprilysin; Peptide Hydrolases; Peptides; Peptidyl-Dipeptidase A; Perfusion; Protease Inhibitors; Ramipril; Rats; Rats, Wistar

1999