Human liver debrisoquine 4-hydroxylase: test for specificity toward various monooxygenase substrates and model of the active site.

Autor: Wolff T, Distlerath LM, Worthington MT, Guengerich FP
Jazyk: angličtina
Zdroj: Archives of toxicology [Arch Toxicol] 1987; Vol. 60 (1-3), pp. 89-90.
DOI: 10.1007/BF00296955
Abstrakt: Polyclonal antibodies raised toward a debrisoquine 4-hydroxylating cytochrome P-450 species purified from rat liver (P-450UT-A) were used to determine which monooxygenase reactions are linked to debrisoquine hydroxylation in human liver. Anti P-450UT-A 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.
Databáze: MEDLINE
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