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Crystallization of cytochrome P-450scc from bovine adrenocortical mitochondria
Y Iwamoto1, M Tsubaki, A Hiwatashi
1Department of Biochemistry, Kagawa Medical School, Japan.
FEBS Letters
|June 6, 1988
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.