Characterization of the liver cytochrome P450 in the marine fish Mugil cephalus and effects of some hydrocarbons on the mixed-function oxidase components

The marine fish Mugil cephalus was caught in the Bay of Marseilles (France) in 1985 and the liver microsomal cytochrome P₄₅₀ was identified at a concentration of about 0.230 nmol mg^-1 protein. Optimal assay conditions were established to measure two mixed-function cytochrome P₄₅₀-dependent oxidases: aniline hydroxylase and p-nitroanisole O-demethylase. Induction of cytochrome P₄₅₀ occurred after exposure of mullet to an aromatic hydrocarbon and a water-soluble petroleum fraction. The liver cytochrome P₄₅₀ was solubilized and purified. The monomer molecular weight of partially purified cytochrome P₄₅₀, determined by sodium dodecyl-sulfate-gel electrophoresis, was 51 000.