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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1990-3-5
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pubmed:abstractText |
The ability of rabbit liver microsomes to 4-hydroxylate phenytoin to 5-(4-hydroxyphenyl)-5-phenylhydantoin was studied. No significant difference was observed between the capacity of control and rifampicin, phenobarbital, acetone, 2,3,7,8-tetrachlorodibenzo-p-dioxin and phenytoin induced rabbit liver microsomes to 4-hydroxylate phenytoin. In reconstitution experiments using six purified rabbit cytochromes P450 isozymes, only P450IIC3 was capable of 4-hydroxylating phenytoin whereas P450IA1, P450IA2, P450IIB4, P450IIIA6, and P450IVB1 were inactive. Further, anti-P450IIC3 IgG completely inhibited phenytoin 4-hydroxylase activity in rabbit liver microsomes. The above data suggest a major role for the constitutive isozyme P450IIC3 in phenytoin 4-hydroxylase activity in rabbit liver. In human liver microsomes P450IIC3 IgG inhibited phenytoin 4-hydroxylase activity by 66%, suggesting that an ortholog to rabbit P450IIC3 is in part responsible for this activity in man.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
166
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
860-6
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:2405858-Animals,
pubmed-meshheading:2405858-Cytochrome P-450 Enzyme System,
pubmed-meshheading:2405858-Humans,
pubmed-meshheading:2405858-Hydroxylation,
pubmed-meshheading:2405858-Immunologic Techniques,
pubmed-meshheading:2405858-Isoenzymes,
pubmed-meshheading:2405858-Microsomes, Liver,
pubmed-meshheading:2405858-Phenytoin,
pubmed-meshheading:2405858-Rabbits,
pubmed-meshheading:2405858-Species Specificity,
pubmed-meshheading:2405858-Substrate Specificity
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pubmed:year |
1990
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pubmed:articleTitle |
Phenytoin 4-hydroxylation by rabbit liver P450IIC3 and identification of orthologs in human liver microsomes.
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pubmed:affiliation |
School of Pharmacy, South Australian Institute of Technology, Adelaide.
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pubmed:publicationType |
Journal Article
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