Biotransformation of glyceryl trinitrate by rat aortic cytochrome P450
BJ McDonald, BM Bennett - Biochemical pharmacology, 1993 - Elsevier
BJ McDonald, BM Bennett
Biochemical pharmacology, 1993•ElsevierDenitration of glyceryl trinitrate (GTN) by the microsomal fraction of rat aorta was found to be
NADPH dependent and followed apparent first-order kinetics (T 1 2 70.1 min).
Biotransformation of GTN was regioselective for glyceryl-1, 2-dinitrate formation, and was
inhibited by carbon monoxide, SKF-525A, and oxygen. In aortic microsomes prepared from
phenobarbital-pretreated rats, biotransfonnation was increased 7-fold, and was
regioselective for glyceryl-1, 3-dinitrate formation. These data strongly suggest the …
NADPH dependent and followed apparent first-order kinetics (T 1 2 70.1 min).
Biotransformation of GTN was regioselective for glyceryl-1, 2-dinitrate formation, and was
inhibited by carbon monoxide, SKF-525A, and oxygen. In aortic microsomes prepared from
phenobarbital-pretreated rats, biotransfonnation was increased 7-fold, and was
regioselective for glyceryl-1, 3-dinitrate formation. These data strongly suggest the …
Denitration of glyceryl trinitrate (GTN) by the microsomal fraction of rat aorta was found to be NADPH dependent and followed apparent first-order kinetics (T 1 2 70.1 min). Biotransformation of GTN was regioselective for glyceryl-1, 2-dinitrate formation, and was inhibited by carbon monoxide, SKF-525A, and oxygen. In aortic microsomes prepared from phenobarbital-pretreated rats, biotransfonnation was increased 7-fold, and was regioselective for glyceryl-1, 3-dinitrate formation. These data strongly suggest the involvement of aortic cytochrome P450 in the biotransformation of GTN.
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