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- W1964983968 abstract "CYP3A4 represents the most important form of human cytochrome P450 active in drug metabolism. Reconstitution of this enzyme has in the past been a major problem. Using purified cDNA-expressed CYP3A4 incorporated into membranous vesicles made from microsomal phospholipids, rates of nifedipine and testosterone oxidation of about 60 nmol/nmol P450/min were achieved, whereas similar reconstitution into dilauroyl-phosphatidylcholine micelles was unsuccessful. A higherVmaxfor nifedipine oxidation was obtained in negatively charged vesicles as compared to neutral membranes, whereas the membrane charge did not influence theKm.It is concluded that the native function of CYP3A4 requires a negatively charged microsomal membrane." @default.
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- W1964983968 date "1996-04-01" @default.
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- W1964983968 title "High Rates of Substrate Hydroxylation by Human Cytochrome P450 3A4 in Reconstituted Membranous Vesicles: Influence of Membrane Charge" @default.
- W1964983968 doi "https://doi.org/10.1006/bbrc.1996.0593" @default.
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