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40
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Text
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n/a
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Pages
688-692
Issue
5
Volume
22
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Title
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CDNA-DIRECTED EXPRESSION OF HUMAN CYTOCHROME-P450 CYP3A4 USING BACULOVIRUS
Publisher
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Drug Metabolism and Disposition
Date
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1994
1994-09
Subject
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pharmacokinetics; Pharmacology & Pharmacy; metabolism; polymorphism; identification; reductase; oxidation; vaccinia virus; human-liver; catalytic activities; hydroxylation
Creator
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Buters J T M; Korzekwa K R; Kunze K L; Omata Y; Hardwick J P; Gonzalez F J
Description
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A recombinant baculovirus containing the human CYP3A4 cDNA was constructed and used to express CYP3A4 in SF9 insect cells (0.46 +/- 0.13 nmol/mg protein, 103 +/- 29 nmol/liter, N = 15). The enzyme represented similar to 2-3% of total cellular protein and could be purified by a two column procedure to a specific content of 12.7 nmol/mg protein. Catalytic activity of the purified enzyme after reconstitution was optimum using molar ratios of CYP3A4 to cytochrome b(5) to NADPH-P450 oxidoreductase of 1:3:20, respectively. The enzyme metabolized cortisol, erythromycin, testosterone, and (R)-warfarin. Recombinant baculovirus expresses the highest amounts of all expression systems published to date of catalytically intact CYP3A4. This system is an excellent alternative for the isolation and characterization of P450 forms from human liver.
Identifier
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n/a
Format
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Journal Article or Conference Abstract Publication
1994
Buters J T M
catalytic activities
Drug Metabolism and Disposition
Gonzalez F J
Hardwick J P
human-liver
Hydroxylation
identification
Journal Article or Conference Abstract Publication
Korzekwa K R
Kunze K L
Metabolism
Omata Y
oxidation
pharmacokinetics
Pharmacology & Pharmacy
Polymorphism
reductase
vaccinia virus