PMID: 8958150Jan 1, 1997Paper

Localization of superoxide dismutase activity in rat tissues

Free Radical Biology & Medicine
W M Frederiks, K S Bosch

Abstract

Superoxide anion radicals have been implicated in a variety of pathological processes. Under physiological conditions, superoxide dismutase (SOD) is effectively able to disproportionate superoxide anions into hydrogen peroxide and dioxygen. Until now, no techniques have been available to localize SOD activity within tissues. In the present study, SOD activity was detected in different rat tissues using a thin film of xanthine oxidase between the glass slide and the unfixed cryostat section and a medium containing hypoxanthine as a source of electrons for the production of superoxide anions. The incubation medium also contained cerium ions to precipitate the hydrogen peroxide product and polyvinyl alcohol to prevent leakage of soluble and/or loosely bound enzymes from the sections into the incubation medium. The cerium perhydroxides that are formed were visualized for the light microscope in a second step using an incubation medium consisting of 3,3'-diaminobenzidine, cobalt ions, and hydrogen peroxide, which results in oxidation of the diaminobenzidine to the final insoluble blue reaction product. By this methodology, high enzyme activity was found not only in endothelial cells of liver and kidney but also in hepatocytes of liv...Continue Reading

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Citations

Dec 31, 2003·The Journal of Surgical Research·Ruey-Hwa LuLih-Min Tsai
Jan 1, 1997·Free Radical Biology & Medicine·B E Van DrielC J Van Noorden
Jan 12, 2013·Antioxidants & Redox Signaling·Dorottya K de VriesJan H N Lindeman
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Feb 13, 2007·Acta Cirúrgica Brasileira·Eva Glória Abrão Siufi do AmaralCelso Massachi Inouye
Jan 6, 2000·Archives of Biochemistry and Biophysics·A D de Grey

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