[Mechanisms of the phenazepam oxidation reactions in cell membranes].
During phenazepam oxidation by rat, mouse and rabbit liver microsomes, the maximal amount of products was formed if NADP-H was used as electron donor. Addition of equimolar concentration of NAD-H did not stimulate phenazepam oxidation. The monooxygenase inhibitor, SKF-525A, reduced the rate of phenazepam oxidation depending on the type of experimental animals. The mechanisms of enzymatic formation from phenazepam of 3-hydroxymetabolite, quinazoline and aromatic hydroxylation products are discussed.
D000693:Anaerobiosis / Q000187:drug effects; D000818:Animals; D014151:Anti-Anxiety Agents / Q000378:metabolism*; D001569:Benzodiazepines; D001570:Benzodiazepinones / Q000378:metabolism*; D004579:Electron Transport / Q000187:drug effects; D007425:Intracellular Membranes / Q000187:drug effects / Q000378:metabolism*; D008297:Male; D051379:Mice; D008808:Mice, Inbred CBA; D008862:Microsomes, Liver / Q000187:drug effects / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction / Q000187:drug effects; D011335:Proadifen / Q000494:pharmacology; D011817:Rabbits; D051381:Rats; D011919:Rats, Inbred Strains
D014151:Anti-Anxiety Agents; D001570:Benzodiazepinones; D009243:NAD; D001569:Benzodiazepines; C017928:phenazepam; D009249:NADP; D011335:Proadifen
Mekhanizmy reaktsiĭ okisleniia fenazepama v tsitomembranakh.