The release of kininase from rat isolated hearts during myocardial ischaemia.
BK destroying activity was observed in rat isolated heart perfusates. BK was optimally degraded at pH 8.4 in rat heart. The results indicated that myocardial kinin degradation was due to ACE and a serine protease. These results suggest that bradykinin may have some cardioprotective role during myocardial ischaemia at acidic pH.
Ahmad
M
M
Department of Physiology and Pharmacology, University of Strathclyde, Glasgow, Scotland, UK.
Zeitlin
I J
IJ
Parratt
J R
JR
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000494:pharmacology; D000818:Animals; D007611:Aprotinin / Q000494:pharmacology; D001920:Bradykinin / Q000378:metabolism; D002216:Captopril / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D001121:Lysine Carboxypeptidase / Q000378:metabolism*; D008297:Male; D017202:Myocardial Ischemia / Q000201:enzymology*; D009206:Myocardium / Q000201:enzymology*; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D010477:Perfusion; D051381:Rats; D017207:Rats, Sprague-Dawley; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology
D000806:Angiotensin-Converting Enzyme Inhibitors; D015842:Serine Proteinase Inhibitors; D007611:Aprotinin; D004492:Edetic Acid; D002216:Captopril; D007703:Peptidyl-Dipeptidase A; D001121:Lysine Carboxypeptidase; D001920:Bradykinin