| pubmed-article:1883820 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1883820 | lifeskim:mentions | umls-concept:C0205054 | lld:lifeskim |
| pubmed-article:1883820 | lifeskim:mentions | umls-concept:C0039601 | lld:lifeskim |
| pubmed-article:1883820 | lifeskim:mentions | umls-concept:C0010762 | lld:lifeskim |
| pubmed-article:1883820 | lifeskim:mentions | umls-concept:C0521451 | lld:lifeskim |
| pubmed-article:1883820 | lifeskim:mentions | umls-concept:C0441889 | lld:lifeskim |
| pubmed-article:1883820 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:1883820 | lifeskim:mentions | umls-concept:C0443264 | lld:lifeskim |
| pubmed-article:1883820 | pubmed:issue | 34 | lld:pubmed |
| pubmed-article:1883820 | pubmed:dateCreated | 1991-10-4 | lld:pubmed |
| pubmed-article:1883820 | pubmed:abstractText | Polyclonal antibody to mitochondrial P-450c27/25 reacted with two proteins of apparent molecular masses of 52 kilodaltons (kDa) and 50 kDa from the female rat liver mitochondrial proteins bound to an omega-octylaminoagarose column. The two proteins were purified to greater than 85% homogeneity by DEAE-Sephacel and hydroxylapatite column chromatography, and both were found to be P-450 as judged by dithionite-reduced CO difference spectra. Both of the P-450 forms required mitochondrial-specific ferredoxin and ferredoxin reductase for in vitro reconstitution of enzyme activities, suggesting that they are mitochondrial forms. The 52-kDa P-450 exhibited the properties of mitochondrial 27/25-hydroxylase with respect to high vitamin D3 25-hydroxylase activity [1.4 nmol (nmol of P-450)-1 min-1] and N-terminal amino acid sequence. The 50-kDa P-450, on the other hand, lacked significant vitamin D3 25-hydroxylase activity, but showed 17 beta-reductase [0.380-0.400 nmol (nmol of P-450)-1 min-1] and 17 beta-oxidase [0.1-0.16 nmol (nmol of P-450)-1 min-1] activities with both androgens and estrogens as substrates. Immunoblot analysis of proteins using a monoclonal antibody specific for P-450c27/25 showed a 2-3-fold higher level of this enzyme in the female liver mitochondria than in the males. Similarly, use of a polyclonal antibody in the immunoblot analysis showed that the 50-kDa P-450 is female-specific. The relative level of P-450c27/25 was reduced significantly in castrated females, while the level of the female-specific 50-kDa P-450 was increased. However, the levels of both enzymes were increased in castrated males.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
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| pubmed-article:1883820 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1883820 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1883820 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1883820 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1883820 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1883820 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1883820 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:1883820 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:1883820 | pubmed:author | pubmed-author:YehY SYS | lld:pubmed |
| pubmed-article:1883820 | pubmed:author | pubmed-author:AvadhaniN GNG | lld:pubmed |
| pubmed-article:1883820 | pubmed:author | pubmed-author:ZhengY MYM | lld:pubmed |
| pubmed-article:1883820 | pubmed:author | pubmed-author:AddyaSS | lld:pubmed |
| pubmed-article:1883820 | pubmed:author | pubmed-author:ShayiqR MRM | lld:pubmed |
| pubmed-article:1883820 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1883820 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:1883820 | pubmed:volume | 30 | lld:pubmed |
| pubmed-article:1883820 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1883820 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1883820 | pubmed:pagination | 8323-30 | lld:pubmed |
| pubmed-article:1883820 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:1883820 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1883820 | pubmed:articleTitle | Characterization of a female-specific hepatic mitochondrial cytochrome P-450 whose steady-state level is modulated by testosterone. | lld:pubmed |
| pubmed-article:1883820 | pubmed:affiliation | Department of Animal Biology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia 19104-6048. | lld:pubmed |
| pubmed-article:1883820 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1883820 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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