Studies on Tetrahymena microsomal electron transport systems: solubilization of microsomal electron transport enzymes involved in fatty acid desaturation.
Tetrahymena microsomes were solubilized with five different detergents and the effect on electron transport enzymes involved in fatty acid desaturation was studied. Cytochrome b560ms and NADPH-cytochrome c reductase were solubilized with a low concentration detergent (0.25%), in the order of sodium deoxycholate greater than Renex 690 greater than Triton X-100 greater than octylglucoside greater than sodium cholate, whereas all of these detergents at the high concentration (1%) could solubilize preferentially both enzymes (70-100%). Increasing the concentration of various detergents from 0.5 to 1.0% did not produce an incremental change in NADH-ferricyanide reductase solubilization. NADH-cytochrome c reductase system, which would be catalyzed by the cooperation action of NADH-ferricyanide and cytochrome b560ms, was relatively inactivated by all detergents. Compared to the other four detergents, octylglucoside has a much higher recovery of stearoyl-CoA desaturase activities in the supernatant. Our study suggests that octylglucoside may be more useful for the isolation in active form of cyanide-sensitive factor (CSF) from Tetrahymena microsomes.
D000818:Animals; D003573:Cytochrome b Group / Q000378:metabolism; D003902:Detergents / Q000494:pharmacology; D004579:Electron Transport; D044943:Fatty Acid Desaturases / Q000378:metabolism*; D008861:Microsomes / Q000201:enzymology*; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism; D013769:Tetrahymena pyriformis / Q000201:enzymology*
D003573:Cytochrome b Group; D003902:Detergents; D044943:Fatty Acid Desaturases; D009247:NADH, NADPH Oxidoreductases