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Microsomal monooxygenase system in frog livers.

M Noshiro, T Omura

    Comparative Biochemistry and Physiology. B, Comparative Biochemistry
    |January 1, 1984
    PubMed
    Summary

    Frog liver microsomes contain cytochrome P-450 and exhibit significant NAD(P)H-dependent monooxygenase activities. These activities vary by species and show distinct responses to chemical compounds compared to rat liver microsomes.

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    Area of Science:

    • Biochemistry
    • Comparative Toxicology
    • Pharmacology

    Background:

    • Cytochrome P-450 enzymes are crucial for metabolizing foreign compounds in vertebrates.
    • Understanding xenobiotic metabolism in amphibians is important for ecotoxicology and comparative studies.
    • Previous research has established monooxygenase activity in various vertebrate liver microsomes.

    Purpose of the Study:

    • To investigate and compare the NAD(P)H-dependent monooxygenase activities of liver microsomes from four different frog species.
    • To characterize the substrate specificity and inducibility of these enzymes.
    • To assess the sensitivity of frog liver monooxygenases to inhibitors like cyanide.

    Main Methods:

    • Preparation of liver microsomes from Rana catesbeiana, Rana nigromaculata, Bufo bufo japonicus, and Xenopus laevis.
    • Assay of NAD(P)H-dependent monooxygenase activities using model substrates like 7-ethoxycoumarin and benzo(a)pyrene.
    • Administration of 3-methylcholanthrene to induce enzyme activity.
    • Evaluation of enzyme inhibition using cyanide.

    Main Results:

    • All four frog species' liver microsomes contained cytochrome P-450 and exhibited NAD(P)H-dependent monooxygenase activities.
    • Significant interspecies variations in the oxidation of tested chemical compounds were observed.
    • Oxidation of 7-ethoxycoumarin was notably faster in frog microsomes than in rat liver microsomes.
    • Benzo(a)pyrene oxidation was significantly induced by 3-methylcholanthrene.
    • Frog liver monooxygenase activities were more sensitive to cyanide inhibition compared to rat liver microsomes.

    Conclusions:

    • Frog liver microsomes possess functional cytochrome P-450-mediated monooxygenase systems with species-specific characteristics.
    • These systems exhibit unique metabolic profiles and sensitivities to induction and inhibition, differing from mammalian models.
    • The findings highlight the potential of amphibians as models for comparative xenobiotic metabolism research.

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