Purification of cytochrome P-450 from bovine adrenocortical mitochondria by an “Aniline-sepharose” and the properties*
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Early years of oxygenase research in Bethesda, Osaka, Urbana, and Kanazawa
2005, Biochemical and Biophysical Research CommunicationsCitation Excerpt :On SDS–polyacrylamide gel electrophoresis, only one protein band for each purified preparation was observed, indicating that the two P450 preparations had been satisfactorily separated in purified forms for further characterization. When the preparations were carboxymethylated in the presence of 6 M guanidine HCl and 100 mM 2-mercaptoethanol, the sedimentation equilibrium data gave molecular weights of 46,000 and 43,000 for P450scc and P45011β, respectively [25,26]. Under a newly developed sensitive assay system, the purified P450scc preparation specifically catalyzed the side-chain cleavage of cholesterol to form pregnenolone with a turnover number of 16 min−1 in the presence of adrenodoxin and NADPH-adrenodoxin reductase, but did not catalyze 11β- or 18-hydroxylase activity for deoxycorticosterone.
A simple and rapid method to measure cholesterol binding to P450s and other proteins
2005, Journal of Lipid ResearchIsolation and partial characterization of a cytochrome P-450 isoenzyme (cytochrome P-450<inf>tu</inf>) from mouse liver tumors
1990, Biochimica et Biophysica Acta (BBA)/Protein Structure and MolecularExistence of multiple forms of cytochrome P-450<inf>scc</inf> purified from bovine adrenocortical mitochondria
1987, Biochimica et Biophysica Acta (BBA)/Protein Structure and MolecularStructure of genes encoding steroidogenic enzymes
1987, Journal of Steroid Biochemistry
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A part of the results was presented at the meeting of International Congress of Biochemistry in Stockholm 1973(1). This work was supported by the Scientific Research Fund B-947051 from the Ministry of Education of Japan.
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Present addresses: Central Research Institute, Suntory Ltd., Osaka 618.
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Present addresses: Research Laboratories, Fujisawa Pharmaceutical Co. Ltd., Osaka 532.