Interaction of cytochrome P-450scc with cytochrome b5.
Spectrophotometric, affinity chromatography and cross-linking experiments provided evidence that cytochrome P-450scc from bovine adrenocortical mitochondria forms a tight complex with cytochrome b5 from rabbit liver microsomes. In the reconstituted system cholesterol side chain activity of cytochrome P-450scc was enhanced by the addition of cytochrome b5.
Usanov
S A
SA
Institute of Bioorganic Chemistry, BSSR Academy of Sciences, Minsk, USSR.
Chashchin
V L
VL
D000302:Adrenal Cortex / Q000378:metabolism; D000325:Adrenodoxin / Q000378:metabolism; D000818:Animals; D002417:Cattle; D002786:Cholesterol Side-Chain Cleavage Enzyme / Q000378:metabolism*; D002846:Chromatography, Affinity; D003432:Cross-Linking Reagents; D015786:Cytochromes b5 / Q000378:metabolism*; D066298:In Vitro Techniques; D008862:Microsomes, Liver / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D011485:Protein Binding; D011817:Rabbits; D013057:Spectrum Analysis
D003432:Cross-Linking Reagents; D000325:Adrenodoxin; D015786:Cytochromes b5; D002786:Cholesterol Side-Chain Cleavage Enzyme