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- W944209541 abstract "During the past few decades, a large accumulated body of experimental data has indicated that the biological reduction of molecular oxygen can yield dangerously reactive free radicals. About 2–5% of the electron, flow in isolated brain mitochondria produces superoxide (O2· –) and hydrogen peroxide (H2O2). These constantly produced oxygen radicals are scavenged by endogenous antioxidants including antioxidative enzymes such as superoxide dismutases (SODS), catalase, glutathione peroxidase, and non-enzymatic antioxidants such as reduced glutathione, ascorbic acid and α-tocopherol. Superoxide dismutase scavenges superoxide radicals at a rate close to diffusion, whereas glutathione peroxidase and catalase are specific scavengers for H2O2 and other lipid peroxides. Both enzymatic and non-enzymatic antioxidants are located in cellular membranes, cytoplasmic compartments and subcellular organelles such as mitochondria and peroxisomes. Based on the metal ion requirements and the anatomical distribution, two types of SOD exist in brain cells. CuZn-SOD is a cytosolic enzyme that requires both copper and zinc ions as cofactors, whereas manganese (Mn)-SOD is a mitochondria1 enzyme with requirement for Mn2+. Recent studies have demonstrated that CuZn-SOD is primarily localized in peroxisomes, a subcellular organelle that also contains high levels of catalase in plants. Both CuZn-SOD and Mn-SOD from various sources have been fully characterized biochemically and the cDNAs of both human enzymes have been successfully cloned. Both cDNA and genomic DNA of human CuZn-SOD have been used to successfully generate transgenic mice." @default.
- W944209541 created "2016-06-24" @default.
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- W944209541 date "1993-01-01" @default.
- W944209541 modified "2023-10-13" @default.
- W944209541 title "Chapter 6 Role of superoxide dismutase in ischemic brain injury: reduction of edema and infarction in transgenic mice following focal cerebral ischemia" @default.
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- W944209541 doi "https://doi.org/10.1016/s0079-6123(08)63260-4" @default.
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