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http://purl.uniprot.org/citations/7948001http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7948001http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7948001http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/7948001http://purl.org/dc/terms/identifier"doi:10.1016/0005-2760(94)90108-2"xsd:string
http://purl.uniprot.org/citations/7948001http://purl.org/dc/terms/identifier"doi:10.1016/0005-2760(94)90108-2"xsd:string
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/author"Hori H."xsd:string
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/author"Hori H."xsd:string
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/author"Ichikawa Y."xsd:string
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/author"Ichikawa Y."xsd:string
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/author"Tsubaki M."xsd:string
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/author"Tsubaki M."xsd:string
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/author"Miyatake A."xsd:string
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/author"Miyatake A."xsd:string
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/pages"176-182"xsd:string
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/pages"176-182"xsd:string
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/title"Purification and comparative characterization of cytochrome P-450scc (CYP XIA1) from sheep adrenocortical mitochondria."xsd:string
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/title"Purification and comparative characterization of cytochrome P-450scc (CYP XIA1) from sheep adrenocortical mitochondria."xsd:string
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/volume"1215"xsd:string
http://purl.uniprot.org/citations/7948001http://purl.uniprot.org/core/volume"1215"xsd:string
http://purl.uniprot.org/citations/7948001http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7948001
http://purl.uniprot.org/citations/7948001http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7948001