Abstract
Polyclonal antibodies raised toward a debrisoquine 4-hydroxylating cytochrome P-450 species purified from rat liver (P-450UTA) were used to determine which monooxygenase reactions are linked to debrisoquine hydroxylation in human liver. Anti P-450UTA did not inhibit the oxidation of dimethylnitrosamine, morphine, diazepam, vinylidene chloride, trichloroethylene, benzo(a)pyrene and its 7.8-dihydrodiol, but was inhibitory for the hydroxylation of debrisoquine, (±)-bufuralol, lasiocarpine and monocrotaline. A model interpreting the substrate specificity of the human liver enzyme is presented.
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Dedicated to Professor Dr. med. Herbert Remmer on the occasion of his 65th birthday
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Wolff, T., Distlerath, L.M., Worthington, M.T. et al. Human liver debrisoquine 4-hydroxylase: test for specifity toward various monooxygenase substrates and model of the active site. Arch Toxicol 60, 89–90 (1987). https://doi.org/10.1007/BF00296955
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DOI: https://doi.org/10.1007/BF00296955