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- W1969971243 abstract "The hydroxylation of amphetamine to p-hydroxyamphetamine has been investigated. In 1 hr, perfused rat livers hydroxylated about 85 per cent of the administered 20 μmole dose of amphetamine. Ninety-four per cent of the p-hydroxyamphetamine was further metabolized by conjugation. Isolated hepatocytes are capable of hydroxylation of amphetamine and conjugation of hydroxyamphetamine at rates comparable to those of the perfused liver. The rate of hydroxylation with microsomes is about 50 per cent of that attained with isolated hepatocytes. With hepatocytes, the hydroxylation is inhibited by typical inhibitors of microsomal oxygenase(s) such as 2,6-dichlorophenyphenoxyethylamine (DPEA) and SKF525A, and it is inhibited by iprindole. However, the rate could not be increased by treatments which induce cytochrome P450 and increase other mono-oxygenase reactions. The results obtained with both isolated hepatocytes and microsomes suggest that amphetamine is hydroxylated by a microsomal cytochrome P450-dependent enzyme system, but that amphetamine is not a typical substrate." @default.
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- W1969971243 date "1978-01-01" @default.
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- W1969971243 title "Aromatic hydroxylation of amphetamine with rat liver microsomes, perfused liver, and isolated hepatocytes" @default.
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- W1969971243 doi "https://doi.org/10.1016/0006-2952(78)90320-9" @default.
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