Superoxide dismutase activity in the cochlea.
It was found that superoxide dismutase (SOD) exhibits a higher specific activity in a fraction of the cochlea that contains the organ of Corti than in most other neural tissues. SOD may comprise as much as 4.3% of the soluble protein in this fraction. Approximately 74% of this SOD is cyanide-inhibitable, indicating that it is the Cu/Zn isoenzyme usually found in the cytoplasm. SOD activity was also found in a fraction containing the stria vascularis. Two enzymes that regulate peroxide concentrations, catalase and glutathione peroxidase, were also prominent in both of these fractions.
D000818:Animals; D002374:Catalase / Q000378:metabolism; D003051:Cochlea / Q000201:enzymology*; D005609:Free Radicals; D005979:Glutathione Peroxidase / Q000378:metabolism; D006168:Guinea Pigs; D009925:Organ of Corti / Q000201:enzymology; D051381:Rats; D013316:Stria Vascularis / Q000201:enzymology; D013482:Superoxide Dismutase / Q000378:metabolism*; D014018:Tissue Distribution
D005609:Free Radicals; D002374:Catalase; D005979:Glutathione Peroxidase; D013482:Superoxide Dismutase