Inhibition of the cytochrome P-450 multifunctional oxidase by N-propargyl analogs of SKF-525 A and acetylmethadol.

New N-propargyl analogs of SKF-525A and acetyl methadol were tested for their inhibitory potency toward P-450 multifunctional oxidase. Metabolism of these analogs appears to be different from the metabolism of SKF-525 A itself; no N-dealkylated species were detected, --in vitro N-demethylation of aminopyrine and spectrofluorometric measurements support the hypothesis of an interaction between the hepatic flavo-protein and the acetylenic function of the inhibitors.