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**Recombinant human copper-zinc superoxide dismutase (rhSOD1)** is a recombinant form of the human SOD1 enzyme, which catalyzes the dismutation of the superoxide radical (\(O_2^{\cdot-}\)) into hydrogen peroxide and molecular oxygen[1][2][4][7]. SOD1 is the primary intracellular antioxidant enzyme, present in the cytoplasm, nucleus, and various organelles. It is a 32 kDa homodimer that uses copper as the redox-active catalytic site and zinc for structural stability[1][2][4]. The drug is produced using recombinant DNA technology (such as expression in E. coli)[7], and acts as an antioxidant enzyme replacement therapy to lower cellular oxidative stress. Its mechanism is relevant to conditions involving excessive oxidative stress or inflammation, such as radiation-induced injury, ischemia-reperfusion injury, and chronic inflammatory states[1][2][3][5][7]. Clinical trials have explored its use for radiation-induced acute rectal injury and respiratory distress in newborns[3].
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