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Spectral metabolic properties of liver microsome from imidazole pre treated rabbits

, : Spectral metabolic properties of liver microsome from imidazole pre treated rabbits. Biochemical & Biophysical Research Communications 108(2): 664-672

Imidazole or phenylimidazole, when administered in vivo, elevates rabbit liver microsomal cytochrome P-450 levels .apprx. 2.0- and 1.5-fold, respectively, as compared to controls. SDS[sodium dodecyl sulfate]-polyacrylamide gel electrophoresis revealed protein bands of enhanced intensity occurring at the approximate positions of LM2, LM3, LM4 and possibly, LM6. Imidazole- and phenylimidazole-induced microsomes exhibit N,N-dimethylaniline and p-nitroanisole demethylase activities which paralleled the increase in cytochrome P-450 content. Dimethylnitrosamine N-demethylase activity, when expressed per nanomole P-450, was 2- to 8-fold greater in imidazole-induced microsomes than in control, phenobarbital- or .beta.-naphthoflavone-induced microsomes, and was inhibited by CO or ethyl isocyanide. Dimethylsulfoxide inhibited dimethylnitrosamine N-demethylase activity 62% in imidazole-induced microsomes, but only 11 and 26% in phenobarbital- or .beta.-naphthoflavone-induced microsomes, respectively. Binding of imidazole to cytochrome P-450 in imidazole-induced microsomes was monophasic, in contrast to the biphasic binding observed in phenobarbital or .beta.-naphthoflavone-induced preparations. The spectral for imidazole binding to imidazole-induced microsomes was 10- to 100-fold less (i.e., 10- to 100-fold greater affinity) than that measured in phenobarbital- or .beta.-naphthoflavone-induced preparations.

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