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- W2000249327 abstract "The antitumor agent, ellipticine (5,11-dimethyl-6H-pyrido[4-3,b]carbazole) is mainly hydroxylated in position 9 by liver microsomes of differently pretreated rats, this result being in agreement with that obtained previously in vivo. A quick and reliable fluorometric assay, based on the differential fluorescent properties of ellipticine and 9-hydroxyellipticine, is described for the measurement of the 9-hydroxylase activity of different microsomes. This activity exhibits the usual features of the cytochrome-P450-dependent monooxygenases. Control rat liver microsomes exhibit a good affinity for ellipticine (Km = 3 × 10−5 M) but a low specific activity (0.1 nmole min−1 mg protein −1), perhaps related with an excess substrate inhibition. Pretreatment of rats with benzo[a]pyrene or ellipticine enhances the rate of 9-hydroxylation: pretreatment with phenobarbital does not. Metyrapone and 7,8 benzofiavone are poor inhibitors of ellipticine hydroxylation particularly in microsomes from benzo[a]pyreneor ellipticine-pretreated rats." @default.
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- W2000249327 date "1977-11-01" @default.
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- W2000249327 title "The hydroxylation of the antitumor agent, ellipticine, by liver microsomes from differently pretreated rats" @default.
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- W2000249327 doi "https://doi.org/10.1016/0006-2952(77)90270-2" @default.
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