| pubmed-article:1726082 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1726082 | lifeskim:mentions | umls-concept:C0020364 | lld:lifeskim |
| pubmed-article:1726082 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:1726082 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:1726082 | lifeskim:mentions | umls-concept:C1710548 | lld:lifeskim |
| pubmed-article:1726082 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:1726082 | pubmed:dateCreated | 1992-6-23 | lld:pubmed |
| pubmed-article:1726082 | pubmed:abstractText | A previously unidentified cytochrome P-450ap possessing the highest aminopyrine-N-demethylase activity has been isolated from liver microsomes of 4-isopropylaminoantipyrine-induced rats, using affinity chromatography in combination with ion-exchange chromatography with subsequent separation on a hydroxyapatite column. The isolated cytochrome P-450ap has the following characteristics: Mr = 49 kD, CO-peak maximum at 450.5 nm, rate of demethylation in a reconstituted system for aminopyrine of 25.5 nmoles of HCHO/min per nmole of P-450, and for benzphetamine a rate of 17.0 nmoles of HCHO/min per nmole of P-450. The hemoprotein synthesis is paralleled by the synthesis of a protein with Mr of 51 kD. Immunochemical analysis permitted the identification of the latter protein as cytochrome P-450b. It was, demonstrated that cytochrome P-450ap does not interact with the antibodies to the major phenobarbital induced form, i.e. with cytochrome P-450b. | lld:pubmed |
| pubmed-article:1726082 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1726082 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1726082 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1726082 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1726082 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1726082 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1726082 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1726082 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1726082 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1726082 | pubmed:issn | 0378-7966 | lld:pubmed |
| pubmed-article:1726082 | pubmed:author | pubmed-author:TsyrlovI BIB | lld:pubmed |
| pubmed-article:1726082 | pubmed:author | pubmed-author:GerasimovK... | lld:pubmed |
| pubmed-article:1726082 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1726082 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:1726082 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1726082 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1726082 | pubmed:pagination | 213-7 | lld:pubmed |
| pubmed-article:1726082 | pubmed:dateRevised | 2011-2-2 | lld:pubmed |
| pubmed-article:1726082 | pubmed:meshHeading | pubmed-meshheading:1726082-... | lld:pubmed |
| pubmed-article:1726082 | pubmed:meshHeading | pubmed-meshheading:1726082-... | lld:pubmed |
| pubmed-article:1726082 | pubmed:meshHeading | pubmed-meshheading:1726082-... | lld:pubmed |
| pubmed-article:1726082 | pubmed:meshHeading | pubmed-meshheading:1726082-... | lld:pubmed |
| pubmed-article:1726082 | pubmed:meshHeading | pubmed-meshheading:1726082-... | lld:pubmed |
| pubmed-article:1726082 | pubmed:meshHeading | pubmed-meshheading:1726082-... | lld:pubmed |
| pubmed-article:1726082 | pubmed:meshHeading | pubmed-meshheading:1726082-... | lld:pubmed |
| pubmed-article:1726082 | pubmed:meshHeading | pubmed-meshheading:1726082-... | lld:pubmed |
| pubmed-article:1726082 | pubmed:meshHeading | pubmed-meshheading:1726082-... | lld:pubmed |
| pubmed-article:1726082 | pubmed:meshHeading | pubmed-meshheading:1726082-... | lld:pubmed |
| pubmed-article:1726082 | pubmed:meshHeading | pubmed-meshheading:1726082-... | lld:pubmed |
| pubmed-article:1726082 | pubmed:meshHeading | pubmed-meshheading:1726082-... | lld:pubmed |
| pubmed-article:1726082 | pubmed:meshHeading | pubmed-meshheading:1726082-... | lld:pubmed |
| pubmed-article:1726082 | pubmed:meshHeading | pubmed-meshheading:1726082-... | lld:pubmed |
| pubmed-article:1726082 | pubmed:articleTitle | Aminopyrine-N-demethylase. II. Characterization of a unique monooxygenase isoform P-450ap. | lld:pubmed |
| pubmed-article:1726082 | pubmed:affiliation | Laboratory of Xenobiochemistry, Academy of Medical Sciences, Siberian Division, Novosibirsk, USSR. | lld:pubmed |
| pubmed-article:1726082 | pubmed:publicationType | Journal Article | lld:pubmed |
