Hydroperoxidation by cytochrome P-450 oxygenase: metabolism of XXXX .

@entity4235 @entity35 @entity167 @entity3209 @entity1110 @entity273 @entity109 @entity72815 @entity72816 @entity72814
@entity72814 was metabolized by @entity35 liver microsomes to @entity72815 and @entity72816 . The results were confirmed by using a reconstituted cytochrome P-450 oxygenase system purified from @entity109 -induced @entity35 liver which established its involvement. SKF-525A strongly inhibited the formation of both oxygenation products. Cytochrome P-450 alone brought about the conversion of the @entity273 to its @entity167 . @entity1110 augmented the peroxidative reaction, but the presence of @entity1110 -cytochrome P-450 reductase was without effect. Certain microsomal preparations and reconstituted enzyme yielded little or no detectable amounts of @entity273 . This was due to a too rapid conversion of the @entity273 to its @entity167 . The addition of @entity4235 , a compound that inhibited such conversion, resulted in accumulation of @entity72815 for positive identification. Incubation of @entity72814 with microsomes and @entity1110 resulted in covalent binding of its metabolite to microsomal proteins. Incubation of @entity3209 -labeled @entity72815 caused covalent binding of label to proteins, RNA, and DNA.
