| pubmed-article:2827463 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2827463 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2827463 | lifeskim:mentions | umls-concept:C0038317 | lld:lifeskim |
| pubmed-article:2827463 | lifeskim:mentions | umls-concept:C0008652 | lld:lifeskim |
| pubmed-article:2827463 | lifeskim:mentions | umls-concept:C0010762 | lld:lifeskim |
| pubmed-article:2827463 | lifeskim:mentions | umls-concept:C0025381 | lld:lifeskim |
| pubmed-article:2827463 | lifeskim:mentions | umls-concept:C0030011 | lld:lifeskim |
| pubmed-article:2827463 | lifeskim:mentions | umls-concept:C0017363 | lld:lifeskim |
| pubmed-article:2827463 | lifeskim:mentions | umls-concept:C0024779 | lld:lifeskim |
| pubmed-article:2827463 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:2827463 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2827463 | pubmed:dateCreated | 1988-2-23 | lld:pubmed |
| pubmed-article:2827463 | pubmed:abstractText | The cytochrome P-450 monooxygenase system possesses catalytic activity toward many exogenous compounds (e.g., drugs, insecticides, and polycyclic aromatic hydrocarbons) and endogenous compounds (e.g., steroids, fatty acids, and prostaglandins). Multiple forms of cytochrome P-450 with different substrate specificities have been isolated. In the present paper we report the isolation and sequence of a cDNA clone for the human hepatic cytochrome P-450 responsible for mephenytoin (an anticonvulsant) oxidation. The mephenytoin cytochrome P-450 is analogous to the rat cytochrome P-450 form termed PB-1 (family P450C2C). We also report that human PB-1 is encoded by one of a small family of related genes all of which map to human chromosome 10q24.1-10q24.3. The endogenous role of this enzyme appears to be in steroid oxidations. This cytochrome P-450 family does not correspond to any of the hepatic cytochrome P-450 gene families previously mapped in humans. | lld:pubmed |
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| pubmed-article:2827463 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2827463 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2827463 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2827463 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2827463 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2827463 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2827463 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:2827463 | pubmed:issn | 0002-9297 | lld:pubmed |
| pubmed-article:2827463 | pubmed:author | pubmed-author:HastieN DND | lld:pubmed |
| pubmed-article:2827463 | pubmed:author | pubmed-author:GosdenJ RJR | lld:pubmed |
| pubmed-article:2827463 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:2827463 | pubmed:author | pubmed-author:FletcherJJ | lld:pubmed |
| pubmed-article:2827463 | pubmed:author | pubmed-author:BucklandRR | lld:pubmed |
| pubmed-article:2827463 | pubmed:author | pubmed-author:FriedbergTT | lld:pubmed |
| pubmed-article:2827463 | pubmed:author | pubmed-author:RoutDD | lld:pubmed |
| pubmed-article:2827463 | pubmed:author | pubmed-author:AdesnikMM | lld:pubmed |
| pubmed-article:2827463 | pubmed:author | pubmed-author:SpurrN KNK | lld:pubmed |
| pubmed-article:2827463 | pubmed:author | pubmed-author:MeehanR RRR | lld:pubmed |
| pubmed-article:2827463 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2827463 | pubmed:volume | 42 | lld:pubmed |
| pubmed-article:2827463 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2827463 | pubmed:authorsComplete | N | lld:pubmed |
| pubmed-article:2827463 | pubmed:pagination | 26-37 | lld:pubmed |
| pubmed-article:2827463 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2827463 | pubmed:meshHeading | pubmed-meshheading:2827463-... | lld:pubmed |
