Purification and some properties of NADPH-cytochrome P-450 reductase from crab-eating monkey liver microsomes |
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| Authors: | S Ohmori M Kitada A Hamada T Igarashi K Ueno Y Kanakubo H Kitagawa |
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| Affiliation: | Faculty of Pharmaceutical Sciences, Chiba University, Japan. |
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| Abstract: | NADPH-cytochrome P-450 reductase was purified to 30.8 units/mg from monkey liver microsomes. The purified reductase showed one major protein band (78,000) and two minor ones (58,000 and 20,000) on analysis by SDS-polyacrylamide gel electrophoresis (SDS-PAGE). Monkey, rat, and guinea pig reductases were not immunochemically identical to each other judged from Ouchterlony double diffusion analysis and immunotitration with regard to NADPH-cytochrome c reductase activity. |
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