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Effects of Enzyme Sources on Midazolam 1-Hydroxylation Activity Catalyzed by Recombinant Cytochrome P450 3A4 in Combination with NADPH-Cytochrome P450 Reductase

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The influence of the enzyme source such as phospholipid and expression ratio of NADPHcytochrome P450 reductase on midazolam 1'-hydroxylation activity of cytochrome P450 3A4 was investigated in reconstituted systems and in membranes using bicistronic expressions. Preferable ratio of P450 reductase over human P450 3A4 would be a determinant factor for the drug metabolism studies.





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Keywords: CYP3A4; E. coli membranes; NADPH-P450 reductase; bicistronic expression; human; lipid mixtures

Document Type: Research Article

Publication date: August 1, 2008

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  • Drug Metabolism Letters publishes short papers on major advances in all areas of drug metabolism and disposition. The emphasis will be on publishing quality papers very rapidly. Letters will be processed rapidly by taking full advantage of the Internet technology for both the submission and review of manuscripts. The journal covers the following areas:

    In vitro systems including CYP-450; enzyme induction and inhibition; drug-drug interactions and enzyme kinetics; pharmacokinetics, toxicokinetics, species scaling and extrapolations; P-glycoprotein and transport carriers; target organ toxicity and interindividual variability; drug metabolism and disposition studies; extrahepatic metabolism; phase I and phase II metabolism; recent developments for the identification of drug metabolites, reactive intermediate and glutathione conjugates.
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