title: Purification and some properties of NADPH-cytochrome P-450 reductase from crab-eating monkey liver microsomes.
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.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D006168:Guinea Pigs; D007120:Immunochemistry; D008251:Macaca / Q000378:metabolism*; D008252:Macaca fascicularis / Q000378:metabolism*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D009251:NADPH-Ferrihemoprotein Reductase / Q000276:immunology / Q000302:isolation & purification*; D051381:Rats; D013045:Species Specificity; D013552:Swine
chemical_list: D000596:Amino Acids; D009251:NADPH-Ferrihemoprotein Reductase