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

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Abstract

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.

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Authors and Affiliations

  1. Faculté des Sciences de Luminy, Centre d'Océanologie de Marseille, UA41, F-13288, Marseille Cedex 9, France

    M. Gilewicz, J. R. Guillaume & J. C. Bertrand

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  1. M. Gilewicz
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  2. J. R. Guillaume
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  3. J. C. Bertrand
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Communicated by J. M. Pérès, Marseilles

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Gilewicz, M., Guillaume, J.R. & Bertrand, J.C. Characterization of the liver cytochrome P450 in the marine fish Mugil cephalus and effects of some hydrocarbons on the mixed-function oxidase components. Mar. Biol. 96, 157–162 (1987). https://doi.org/10.1007/BF00427014

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