Crystallization of cytochrome P‐450scc from bovine adrenocortical mitochondria

FEBS Letters

Ichikawa, Yoshiyuki¹  Iwamoto, Yoshiki¹  Tsubaki, Motonari¹  Hiwatashi, Atsuo¹ 

[1] Department of Biochemistry, Kagawa Medical School, Miki-cho, Kita-gun, Kagawa 761-07, Japan

关键词: Cytochrome P-450scc;    Membrane protein;    Crystallization;    Pyridoxal 5′-phosphate;    Glycerol;    Polarization microscope;    P-450scc;    cytochrome P-450scc;    PLP;    pyridoxal 5′-phosphate;    P-450scc-PLP complex;    covalent complex of cytochrome P-450scc with pyridoxal 5′-phosphate;   

DOI  :  10.1016/0014-5793(88)81350-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cytochrome P-450_scc (P-450_scc), 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-450_scc were also obtained by the same procedure. We identified the crystals as the P-450_scc-PLP complex or native P-450_scc by absorption spectroscopy and SDS-polyacrylamide gel electrophoresis, and characterized them under a polarization microscope.

【 授权许可】

Unknown