Purification and properties of the tightly bound reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase of bovine adrenocortical mitochondria.
Two forms of NADPH-adrenodoxin reductase, tightly and loosely bound forms, were found in bovine adrenocortical mitochondria. The loosely bound NADPH-adrenodoxin reductase was solubilized by ultrasonication and its content was about 65% of the total activity in bovine adrenocortical mitochondria. The tightly bound NADPH-adrenodoxin reductase could not be solubilized by mechanical sonication and required detergent treatment. The tightly bound NADPH-adrenodoxin reductase was purified to homogeneity, judging by sodium dodecyl sulfate (SDS) gel electrophoresis, from bovine adrenocortical mitochondria using sodium cholate solubilization and chromatography on DEAE-Sepharose and 2'5'-ADP-Sepharose columns. Its physicochemical properties were similar to those of the loosely bound form, except for its carbohydrate composition.
D000302:Adrenal Cortex / Q000201:enzymology*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002627:Chemistry, Physical; D004591:Electrophoresis, Polyacrylamide Gel; D005287:Ferredoxin-NADP Reductase / Q000302:isolation & purification*; D005415:Flavins / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology*; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification*; D009249:NADP / Q000378:metabolism
D000596:Amino Acids; D002241:Carbohydrates; D005415:Flavins; D009249:NADP; D005287:Ferredoxin-NADP Reductase; D009247:NADH, NADPH Oxidoreductases