| pubmed-article:1690539 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1690539 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:1690539 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:1690539 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:1690539 | lifeskim:mentions | umls-concept:C0003241 | lld:lifeskim |
| pubmed-article:1690539 | lifeskim:mentions | umls-concept:C0010798 | lld:lifeskim |
| pubmed-article:1690539 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:1690539 | lifeskim:mentions | umls-concept:C0243102 | lld:lifeskim |
| pubmed-article:1690539 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
| pubmed-article:1690539 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:1690539 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1690539 | pubmed:dateCreated | 1990-4-26 | lld:pubmed |
| pubmed-article:1690539 | pubmed:abstractText | An anti-peptide antibody has been produced which binds to and specifically inhibits the activity of cytochrome P-450IA2 in rat hepatic microsomes. This was achieved by raising an antibody against a synthetic peptide (Ser-Glu-Asn-Tyr-Lys-Asp-Asn), the sequence of which occurs in cytochrome P-450IA2 at positions 290-296. The selection of this region of cytochrome P-450IA2 was based on several criteria, including prediction of surface and loop areas, identification of variable regions between cytochromes P-450IA2 and P-450IA1, and consideration of a site on cytochrome P-450IA1 where chemical modification has been shown to cause substantial enzyme inactivation. The specificity of antibody binding was determined by enzyme-linked immunosorbent assay and by immunoblotting using hepatic microsomal preparations and purified cytochrome P-450 isoenzymes. This showed that the antibody binds specifically to rat and mouse cytochrome P-450IA2 and to no other cytochrome P-450, as was predicted from the amino acid sequences of the peptide and the cytochromes P-450. The effect of the antibody upon enzyme activity was studied in hepatic microsomes from rats treated with 3-methylcholanthrene. The antibody was shown to inhibit specifically the activity of reactions catalysed by cytochrome P-450IA2 (phenacetin O-de-ethylase and 2-acetylaminofluorene activation), but had no effect on aryl hydrocarbon hydroxylase activity, which is catalysed by cytochrome P-450IA1, or on aflatoxin B1 activation. | lld:pubmed |
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| pubmed-article:1690539 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1690539 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1690539 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1690539 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1690539 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1690539 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:1690539 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:1690539 | pubmed:author | pubmed-author:BoobisA RAR | lld:pubmed |
| pubmed-article:1690539 | pubmed:author | pubmed-author:DaviesD SDS | lld:pubmed |
| pubmed-article:1690539 | pubmed:author | pubmed-author:EdwardsR JRJ | lld:pubmed |
| pubmed-article:1690539 | pubmed:author | pubmed-author:MurrayB PBP | lld:pubmed |
| pubmed-article:1690539 | pubmed:author | pubmed-author:SesardicDD | lld:pubmed |
| pubmed-article:1690539 | pubmed:author | pubmed-author:SingletonA... | lld:pubmed |
| pubmed-article:1690539 | pubmed:author | pubmed-author:RichK JKJ | lld:pubmed |
| pubmed-article:1690539 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1690539 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1690539 | pubmed:volume | 266 | lld:pubmed |
| pubmed-article:1690539 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1690539 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1690539 | pubmed:pagination | 497-504 | lld:pubmed |
| pubmed-article:1690539 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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