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Superoxide dismutase (SOD) is the only antioxidant enzyme that scavenges the superoxide anion by converting this free radical to oxygen and hydrogen peroxide, thus preventing peroxynitrite production and further damage.
Superoxide dismutase (SOD) catalyzes the removal of the O2- free radical. The enzyme protects oxygen-metabolizing cells against harmful effects of superoxide free-radicals. Superoxide dismutase is inactivated by H2O2. It consists of two subunits of identical molecular weight joined by a disulfide bond.
Superoxide dismutase from bovine erythrocytes has been used in a study to assess a kinetic model of radiation-induced inactivation of superoxide dismutase in nitrous oxide-saturated solutions. Superoxide dismutase from bovine erythrocytes has also been used in a study to investigate the possible participation of superoxide anion in the intestinal tryptophan 2,3-dioxygenase reaction.
| CAS Number | 9054-89-1 |
| Form | Solid |
| Storage | -20°C, sealed |
[2] Eva Nozik-Grayck, et al. Int J Biochem Cell Biol. Extracellular superoxide dismutase
[3] Daniel Dive, et al. Redox Rep. Superoxide dismutase in Plasmodium: a current survey
[4] A T Canada, et al. Pharmacol Ther. Superoxide dismutase: its role in xenobiotic detoxification
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