Use of a direct high performance liquid chromatography method for multiple testosterone hydroxylations in studies of microsomal monooxygenase activities

Jm, Tredger; Hm, Smith; Davis, Michael; Williams, Roger L.

doi:10.1016/0006-2952(84)90341-1

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Cited by 12 publications

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Genetically engineered V79 chinese hamster cell expression of purified cytochrome P‐450iib1 monooxygenase activity

Platt

Molitor

Döhmer

et al. 1989

J. Biochem. Toxicol.

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Chinese hamster V79 fibroblasts, frequently used as target cells in short-term tests for mutagenicity, do not possess measurable monooxygenase activity; in particular, enzymatic oxidation of testosterone (T) cannot be demonstrated. If these V79 cells, however, had been transfected with the cDNA-encoding rat liver cytochrome P-450IIB1 under control of the SV40 early promoter, they stably expressed monooxygenase activity. These so-called SD1 cells then oxidatively metabolized T at a rate of 27 pmol/mg protein/min, converting it to 16 alpha- and 16 beta-hydroxy-T as well as 4-androsten-3,17-dione as sole metabolites in a ratio of 1.1:1.0:1.6. The regio- and stereoselective conversion of T by SD1 cells, as well as the quantitative distribution of the metabolites, corresponds well with the results reported for pure cytochrome P-450IIB1 in a reconstituted system.

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