| http://purl.uniprot.org/citations/1910294 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1910294 | http://www.w3.org/2000/01/rdf-schema#comment | "The major polycyclic aromatic hydrocarbon-metabolizing cytochrome P450 in the mouse embryo fibroblast-derived C3H/10T1/2 CL8 cell line (P450-EF) has been partially purified from benz[a]anthracene (BA)-induced 10T1/2 cells (40 pmol P450/mg). The purification of P450-EF was carried out by sequential chromatography of solubilized microsomes over hydrophobic aminohexyl-Sepharose 4B, anion exchange DE-52 cellulose, and cation exchange carboxymethyl trisacryl columns. The final preparation (1700 pmol/mg) appeared as a single major 55-kDa band by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Reconstitution of detergent-free partially purified P450-EF yielded a relatively high turnover for 7,12-dimethylbenz[a]anthracene (DMBA) metabolism (5.4 nmol/nmol/min). Polyclonal antibodies to purified P450-EF (anti-P450-EF), raised in, respectively, rabbit and chicken, detected a single 55-kDa band in 10T1/2 cell microsomes that was highly inducible by BA (approximately 20-fold) and TCDD (approximately 5-fold). Rabbit anti-P450-EF was much more effective than the corresponding chicken antibody at binding denatured P450-EF protein on Western blots. Conversely, only the chicken antibody was effective at inhibiting DMBA metabolism catalyzed by microsomal P450-EF. This antibody did not inhibit P450IA1-mediated DMBA metabolism. Rabbit anti-P450-EF recognized very weakly (less than 1% of homologous protein response) pure P450IA1, IIB1, IIC7, IIE1, and IIIA1 proteins on Western blots but exhibited substantial cross-reactivity (approximately 10%) with pure P450IIA1 and very strong cross-reactivity (approximately 75%) with a hormonally regulated rat adrenal P450. Polyclonal antibodies to several major P450 subfamilies either did not recognize P450-EF (anti-P450IA, IIB, and IIC) or recognized it very weakly (anti-P450IIA1). P450-EF is probably distantly related to the P450IIA subfamily and may belong to a new P450 subfamily."xsd:string |
| http://purl.uniprot.org/citations/1910294 | http://purl.org/dc/terms/identifier | "doi:10.1016/0003-9861(91)90070-y"xsd:string |
| http://purl.uniprot.org/citations/1910294 | http://purl.uniprot.org/core/author | "Jefcoate C.R."xsd:string |
| http://purl.uniprot.org/citations/1910294 | http://purl.uniprot.org/core/author | "Christou M."xsd:string |
| http://purl.uniprot.org/citations/1910294 | http://purl.uniprot.org/core/author | "Pottenger L.H."xsd:string |
| http://purl.uniprot.org/citations/1910294 | http://purl.uniprot.org/core/date | "1991"xsd:gYear |
| http://purl.uniprot.org/citations/1910294 | http://purl.uniprot.org/core/name | "Arch Biochem Biophys"xsd:string |
| http://purl.uniprot.org/citations/1910294 | http://purl.uniprot.org/core/pages | "488-497"xsd:string |
| http://purl.uniprot.org/citations/1910294 | http://purl.uniprot.org/core/title | "Purification and immunological characterization of a novel cytochrome P450 from C3H/10T1/2 cells."xsd:string |
| http://purl.uniprot.org/citations/1910294 | http://purl.uniprot.org/core/volume | "286"xsd:string |
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