pubmed-article:3182866 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3182866 | lifeskim:mentions | umls-concept:C0038317 | lld:lifeskim |
pubmed-article:3182866 | lifeskim:mentions | umls-concept:C0034493 | lld:lifeskim |
pubmed-article:3182866 | lifeskim:mentions | umls-concept:C0010762 | lld:lifeskim |
pubmed-article:3182866 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
pubmed-article:3182866 | lifeskim:mentions | umls-concept:C1446409 | lld:lifeskim |
pubmed-article:3182866 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:3182866 | pubmed:issue | 33 | lld:pubmed |
pubmed-article:3182866 | pubmed:dateCreated | 1988-12-20 | lld:pubmed |
pubmed-article:3182866 | pubmed:abstractText | The binding of the amino steroid, 22-amino-23,24-bisnor-5-cholen-3 beta-ol (22-ABC), to rabbit liver cytochrome P-450 3c was studied using purified P-450 3c and liver microsomes prepared from rifampicin-treated B/J rabbits. 22-ABC binds to purified cytochrome P-450 3c producing a type II spectral change reflecting the coordination of the amine with the heme iron of the protein. In the absence of allosteric effectors, the binding is characterized by a Ks of 5 microM. In the presence of alpha-naphthoflavone or progesterone, the Ks decreases to 0.8 microM, indicating that these two compounds serve as positive effectors of the binding of 22-ABC to cytochrome P-450 3c. The antibiotic rifampicin induces cytochrome P-450 3c in rabbit liver microsomes, and the benzo(a)pyrene hydroxylase, estradiol 2-hydroxylase, and progesterone 6 beta-hydroxylase activities of these microsomes are stimulated by alpha-naphthoflavone. Moreover, the progesterone 6 beta-hydroxylase activity catalyzed by these microsomes exhibits a dependence on substrate concentration that is consistent with activation of the enzyme by the substrate, progesterone. The magnitude of the type II spectral change elicited by 22-ABC for microsomes prepared from rifampicin-treated B/J rabbits is greater than that observed for microsomes from untreated rabbits. For microsomes from rifampicin-treated rabbits, the apparent binding constant for 22-ABC was decreased 5-fold in the presence of alpha-naphthoflavone. We propose that the effects of alpha-naphthoflavone and progesterone on the binding of 22-ABC to cytochrome P-450 3c mimic the effects of the two positive effectors on the metabolism of substrates by increasing the affinity of the enzyme for substrate. | lld:pubmed |
pubmed-article:3182866 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3182866 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3182866 | pubmed:language | eng | lld:pubmed |
pubmed-article:3182866 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3182866 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3182866 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3182866 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3182866 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3182866 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3182866 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3182866 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3182866 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3182866 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3182866 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3182866 | pubmed:month | Nov | lld:pubmed |
pubmed-article:3182866 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:3182866 | pubmed:author | pubmed-author:VickeryL ELE | lld:pubmed |
pubmed-article:3182866 | pubmed:author | pubmed-author:JohnsonE FEF | lld:pubmed |
pubmed-article:3182866 | pubmed:author | pubmed-author:SchwabG EGE | lld:pubmed |
pubmed-article:3182866 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3182866 | pubmed:day | 25 | lld:pubmed |
pubmed-article:3182866 | pubmed:volume | 263 | lld:pubmed |
pubmed-article:3182866 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3182866 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3182866 | pubmed:pagination | 17672-7 | lld:pubmed |
pubmed-article:3182866 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:3182866 | pubmed:meshHeading | pubmed-meshheading:3182866-... | lld:pubmed |
pubmed-article:3182866 | pubmed:year | 1988 | lld:pubmed |
pubmed-article:3182866 | pubmed:articleTitle | Positive effectors of the binding of an active site-directed amino steroid to rabbit cytochrome P-450 3c. | lld:pubmed |
pubmed-article:3182866 | pubmed:affiliation | Department of Basic and Clinical Research, Scripps Clinic and Research Foundation, La Jolla, California 92037. | lld:pubmed |
pubmed-article:3182866 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3182866 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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