Superoxide dismutase-sensitive, NAD(P)H-dependent reduction of oxygen by the membrane-bound redox chains of liver microsomes and hepatoma nuclei in the presence of adrenaline.
Evidence has been obtained that the NAD(P)H-dependent "generation of superoxide radicals" by various types of membrane bound redox chains, as studied by the adrenaline method, does not occur in the absence of adrenaline. Studies of the oxygen uptake associated with the NAD(P)H-dependent adrenaline co-oxidation confirm the presence of an unusual cyanide-sensitive electron transfer system in the nuclear membranes from Hepatoma 22a. This redox chain contains a b-type cytochrome which resembles cytochrome b5.
D000818:Animals; D002467:Cell Nucleus / Q000187:drug effects / Q000378:metabolism*; D004837:Epinephrine / Q000494:pharmacology*; D007700:Kinetics; D008114:Liver Neoplasms, Experimental / Q000378:metabolism*; D008297:Male; D051379:Mice; D008809:Mice, Inbred C3H; D008862:Microsomes, Liver / Q000187:drug effects / Q000378:metabolism*; D009243:NAD / Q000378:metabolism*; D009249:NADP / Q000378:metabolism*; D010084:Oxidation-Reduction; D010101:Oxygen Consumption / Q000187:drug effects*; D013482:Superoxide Dismutase / Q000378:metabolism*
D009243:NAD; D009249:NADP; D013482:Superoxide Dismutase; D004837:Epinephrine