Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
|
pubmed:dateCreated |
1994-12-20
|
pubmed:abstractText |
Cytochrome P-450scc (CYP XI A1) was purified from sheep adrenocortical mitochondria. The purified cytochrome was found to be homogeneous on SDS-polyacrylamide gel electrophoresis and to have a heme content of 20.8 nmol/mg of protein. Its amino acid composition and NH2-terminal amino acid sequence were determined, and compared with those of other known mammalian and fish cytochromes P-450scc. EPR spectra of the cytochrome P-450scc were measured for oxidized and NO-reduced forms in the presence or absence of cholesterol and/or adreno-ferredoxin. Spectral properties of these various forms were very similar to those of the bovine enzyme. Circular dichroism spectra of the purified sheep cytochrome P-450scc in the oxidized and dithionite-reduced forms, and of their complexed forms with cholesterol or adreno-ferredoxin were analyzed in the region from 200 to 700 nm. The difference CD spectrum of the oxidized cytochrome P-450scc complexed with adreno-ferredoxin minus the oxidized form suggests an increase in the high-spin form upon the addition of adreno-ferredoxin. This may suggest a direct influence of the adreno-ferredoxin binding to the heme moiety of the oxidized cytochrome P-450scc.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
0006-3002
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
17
|
pubmed:volume |
1215
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
176-82
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:7948001-Adrenal Cortex,
pubmed-meshheading:7948001-Amino Acid Sequence,
pubmed-meshheading:7948001-Amino Acids,
pubmed-meshheading:7948001-Animals,
pubmed-meshheading:7948001-Cholesterol Side-Chain Cleavage Enzyme,
pubmed-meshheading:7948001-Circular Dichroism,
pubmed-meshheading:7948001-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:7948001-Mitochondria,
pubmed-meshheading:7948001-Molecular Sequence Data,
pubmed-meshheading:7948001-Sheep
|
pubmed:year |
1994
|
pubmed:articleTitle |
Purification and comparative characterization of cytochrome P-450scc (CYP XIA1) from sheep adrenocortical mitochondria.
|
pubmed:affiliation |
Research Equipment Center, Kagawa Medical School, Japan.
|
pubmed:publicationType |
Journal Article,
Comparative Study
|