1
40
2
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
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n/a
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Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
Pages
688-692
Issue
5
Volume
22
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Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
CDNA-DIRECTED EXPRESSION OF HUMAN CYTOCHROME-P450 CYP3A4 USING BACULOVIRUS
Publisher
An entity responsible for making the resource available
Drug Metabolism and Disposition
Date
A point or period of time associated with an event in the lifecycle of the resource
1994
1994-09
Subject
The topic of the resource
pharmacokinetics; Pharmacology & Pharmacy; metabolism; polymorphism; identification; reductase; oxidation; vaccinia virus; human-liver; catalytic activities; hydroxylation
Creator
An entity primarily responsible for making the resource
Buters J T M; Korzekwa K R; Kunze K L; Omata Y; Hardwick J P; Gonzalez F J
Description
An account of the resource
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
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1002/(sici)1098-2744(199612)17:4%3C241::aid-mc8%3E3.0.co;2-g" target="_blank" rel="noreferrer noopener">http://doi.org/10.1002/(sici)1098-2744(199612)17:4%3C241::aid-mc8%3E3.0.co;2-g</a>
Rights
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
Pages
241-249
Issue
4
Volume
17
Search for Full-text
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The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
Specificity of cDNA-expressed human and rodent cytochrome P450s in the oxidative metabolism of the potent carcinogen 7,12-dimethylbenz a anthracene
Publisher
An entity responsible for making the resource available
Molecular Carcinogenesis
Date
A point or period of time associated with an event in the lifecycle of the resource
1996
1996-12
Subject
The topic of the resource
12-dimethylbenz(a)anthracene; 12-dimethylbenz(a)anthracene; 12-dimethylbenzanthracene metabolites; 7; binding; Biochemistry & Molecular Biology; cDNA expression; chromatography; cytochrome P450; high-performance liquid; human-tissues; hydrocarbons; liver; lung-cancer; metabolism of polycyclic aromatic; microsomes; mouse skin; Oncology; purification; rat; vaccinia virus
Creator
An entity primarily responsible for making the resource
Shou M G; Korzekwa K R; Krausz K W; Buters J T M; Grogan J; Goldfarb I; Hardwick J P; Gonzalez F J; Gelboin H V
Description
An account of the resource
7,12-Dimethylbenz[a]anthracene (DMBA), a potent carcinogen, requires metabolic activation by cytochrome P450s (P450s) to electrophilic metabolites that result in DNA modification, mutagenicity, and carcinogenicity. In this study, we used eight human forms, four rodent forms, and one rabbit form of P450 expressed from recombinant vaccinia or baculovirus vectors to define their specificity for metabolizing DMBA. Of the eight human P450s, 1A1 was the most active (specific activity = 14.7 nmol/min/nmol of P450) in total metabolism of DMBA and showed approximately 6- to 33-fold more activity than other P450s. 2B6, 2C9, and 1A2 were also capable of metabolizing DMBA (2.0-2.5 nmol/min/nmol of P450), whereas 2C8, 2E1, 3A4, and 3A5 exhibited relatively low activities. Among animal P450s, mouse 1A1 exhibited activity similar to that of human 1A1 and had 5.0- to 37-fold more activity than other rodent and rabbit P450s. In regard to enzyme regioselectivity, most human and rodent P450s predominantly formed the 8,9-diol, but human 2B6 and rat 2B1 preferentially formed the 5,6-diol. In the production of monohydroxymethyl metabolites, all the enzymes yielded more 7-hydroxymethyl-12-methylbenz[a]anthracene (7HOM12MBA) than 12-hydroxymethyl-7-methylbenz[a]anthracene (7M12HOMBA), except for human 1A1, which presented the reverse selectivity. Human liver microsomes from 10 organ donors were shown to metabolize DM BA and in most circumstances generated the meta belie profile DM BA trans-8,9-d dihydrodiol > 7HOM12MBA greater than or equal to DMBA trans-5,6-dihydrodiol greater than or equal to 7,12-dihydroxymethylbenz[a]anthracene > 7M12HOMBA > DMBA trans-3,4-dihydrodiol. Thus, the combined activity of hepatic microsomal 2C9, 1A2, and 2B6 may contribute to the metabolic activation and the metabolism of DMBA in normal human liver. (C) 1996 Wiley-Liss, Inc.
Identifier
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<a href="http://doi.org/10.1002/(sici)1098-2744(199612)17:4%3C241::aid-mc8%3E3.0.co;2-g" target="_blank" rel="noreferrer noopener">10.1002/(sici)1098-2744(199612)17:4%3C241::aid-mc8%3E3.0.co;2-g</a>
Format
The file format, physical medium, or dimensions of the resource
Journal Article
12-dimethylbenz(a)anthracene
12-dimethylbenzanthracene metabolites
1996
7
Binding
Biochemistry & Molecular Biology
Buters J T M
cDNA expression
Chromatography
cytochrome P450
Gelboin H V
Goldfarb I
Gonzalez F J
Grogan J
Hardwick J P
high-performance liquid
human-tissues
Hydrocarbons
Journal Article
Korzekwa K R
Krausz K W
Liver
lung-cancer
metabolism of polycyclic aromatic
Microsomes
Molecular carcinogenesis
mouse skin
oncology
purification
rat
Shou M G
vaccinia virus