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PB-4 substrate benzphetamine (1mM). Unactivated TID was shown to be an effective inhibitor of P-450-dependent 7-ethoxycoumarin O-deethylation catalyzed by PB-induced liver microsomes (IC/sub 50/ = 10..mu..M at 120..mu..M substrate). TID inhibited purified, reconstituted P-450 PB-4 with kinetics consistent with either competitive or mixed inhibition and a Ki of 2..mu..M. These findings indicate that TID is an active site-directed inhibitor of this hemeprotein and suggest that (/sup 125/I)TID may serve as a useful probe for the substrate binding site of rat hepatic P-450 PB-4.
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CAMILLE KUDRNA (2024) studied this question.
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