Induction of the ethanol-inducible form of rabbit liver microsomal cytochrome P-450 by inhibitors of alcohol dehydrogenase.

Cytochrome P-450 LMeb was purified from liver microsomes obtained from rabbits treated with either benzene or imidazole and was shown to have identical N-terminal amino acid sequence as that of cytochrome P-450 LM3a. The amino acid compositions of the proteins were indistinguishable. Quantitation of P-450 LMeb in various types of microsomes using radial immunodiffusion, revealed that pyrazole- or imidazole-treatment of the animals caused a 2-3-fold induction of the enzyme, accompanied by 2-3-fold increases of the rates of ethanol and aniline oxidation.