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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
34
|
| pubmed:dateCreated |
1991-10-4
|
| 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)
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0006-2960
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
27
|
| pubmed:volume |
30
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
8323-30
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:1883820-Amino Acid Sequence,
pubmed-meshheading:1883820-Animals,
pubmed-meshheading:1883820-Antibodies,
pubmed-meshheading:1883820-Antibodies, Monoclonal,
pubmed-meshheading:1883820-Blotting, Western,
pubmed-meshheading:1883820-Cytochrome P-450 Enzyme System,
pubmed-meshheading:1883820-Dogs,
pubmed-meshheading:1883820-Female,
pubmed-meshheading:1883820-Kinetics,
pubmed-meshheading:1883820-Male,
pubmed-meshheading:1883820-Mice,
pubmed-meshheading:1883820-Mice, Inbred BALB C,
pubmed-meshheading:1883820-Mitochondria, Liver,
pubmed-meshheading:1883820-Molecular Sequence Data,
pubmed-meshheading:1883820-Rats,
pubmed-meshheading:1883820-Rats, Inbred Strains,
pubmed-meshheading:1883820-Sex Characteristics,
pubmed-meshheading:1883820-Substrate Specificity,
pubmed-meshheading:1883820-Testosterone
|
| pubmed:year |
1991
|
| pubmed:articleTitle |
Characterization of a female-specific hepatic mitochondrial cytochrome P-450 whose steady-state level is modulated by testosterone.
|
| pubmed:affiliation |
Department of Animal Biology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia 19104-6048.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|