| pubmed-article:284396 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:284396 | lifeskim:mentions | umls-concept:C0038323 | lld:lifeskim |
| pubmed-article:284396 | lifeskim:mentions | umls-concept:C0010762 | lld:lifeskim |
| pubmed-article:284396 | lifeskim:mentions | umls-concept:C1261381 | lld:lifeskim |
| pubmed-article:284396 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:284396 | lifeskim:mentions | umls-concept:C0018966 | lld:lifeskim |
| pubmed-article:284396 | lifeskim:mentions | umls-concept:C1511539 | lld:lifeskim |
| pubmed-article:284396 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:284396 | pubmed:dateCreated | 1979-5-23 | lld:pubmed |
| pubmed-article:284396 | pubmed:abstractText | The hepatic pigment accumulated as a consequence of the self-catalyzed destruction of cytochrome P-450 by norethisterone (17-hydroxy-19-nor-17 alpha-pregn-4-en-20-yn-3-one), after acidic methylation and purification, consists of two virtually identical, probably isomeric, porphyrins. Radiolabeled norethisterone is incorporated into both porphyrin products. The major of the two porphyrins exhibits a mass spectrometric molecular ion exactly equivalent to the sum of norethisterone and dimethylprotoporphyrin IX, less two hydrogen atoms: unequivocably demonstrating covalent association of the sterol with this porphyrin in a 1:1 ratio. Cytochrome P-450 is therefore destroyed by self-catalyzed addition of norethisterone to its heme prosthetic group. Cytochrome P-450 is also destroyed by norgestrel (13-ethyl-17-hydroxyl-18, 19-dinor-17 alpha-pregn-4-en-20-yn-3-one) and by 1-ethynylcyclohexanol but not by 17-hydroxy-19-nor-17alpha-pregn-4,20-dien-3-one. The destructive potential is thus clearly a property of the propargylic alcohol function. A mechanism involving enzymatic oxidation of the triple bond is postulated. | lld:pubmed |
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| pubmed-article:284396 | pubmed:language | eng | lld:pubmed |
| pubmed-article:284396 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:284396 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:284396 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:284396 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:284396 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:284396 | pubmed:author | pubmed-author:Ortiz de... | lld:pubmed |
| pubmed-article:284396 | pubmed:author | pubmed-author:MicoB ABA | lld:pubmed |
| pubmed-article:284396 | pubmed:author | pubmed-author:YostG SGS | lld:pubmed |
| pubmed-article:284396 | pubmed:author | pubmed-author:KunzeK LKL | lld:pubmed |
| pubmed-article:284396 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:284396 | pubmed:volume | 76 | lld:pubmed |
| pubmed-article:284396 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:284396 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:284396 | pubmed:pagination | 746-9 | lld:pubmed |
| pubmed-article:284396 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:284396 | pubmed:meshHeading | pubmed-meshheading:284396-C... | lld:pubmed |
| pubmed-article:284396 | pubmed:year | 1979 | lld:pubmed |
| pubmed-article:284396 | pubmed:articleTitle | Self-catalyzed destruction of cytochrome P-450: covalent binding of ethynyl sterols to prosthetic heme. | lld:pubmed |
| pubmed-article:284396 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:284396 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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