title: Studies on Tetrahymena microsomal electron transport systems: solubilization of microsomal electron transport enzymes involved in fatty acid desaturation.
abstract: 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.
mesh_terms: 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*
chemical_list: D003573:Cytochrome b Group; D003902:Detergents; D044943:Fatty Acid Desaturases; D009247:NADH, NADPH Oxidoreductases