title: Crystallization of cytochrome P-450scc from bovine adrenocortical mitochondria.
abstract: Cytochrome P-450scc (P-450scc), a cholesterol side-chain cleavage enzyme from bovine adrenocortical mitochondria, has been crystallized for the first time. Upon removal of glycerol from the solution of the native enzyme complexed with pyridoxal 5'-phosphate (PLP) by microdialysis against distilled water, reddish and planar crystals appeared. The crystals of native P-450scc were also obtained by the same procedure. We identified the crystals as the P-450scc-PLP complex or native P-450scc by absorption spectroscopy and SDS-polyacrylamide gel electrophoresis, and characterized them under a polarization microscope.
authors: Department of Biochemistry, Kagawa Medical School, Japan.
authors: Y
authors: Y
authors: Iwamoto
authors: M
authors: M
authors: Tsubaki
authors: A
authors: A
authors: Hiwatashi
authors: Y
authors: Y
authors: Ichikawa
mesh_terms: D000302:Adrenal Cortex / Q000201:enzymology*; D000818:Animals; D002417:Cattle; D002786:Cholesterol Side-Chain Cleavage Enzyme; D003460:Crystallization; D003956:Dialysis; D004591:Electrophoresis, Polyacrylamide Gel; D008859:Microscopy, Polarization; D008928:Mitochondria / Q000201:enzymology; D013053:Spectrophotometry
chemical_list: D002786:Cholesterol Side-Chain Cleavage Enzyme