Description

• General description: Research area: Cell signaling. Superoxide Dismutase (SOD) is found in allaerobic cells of the animals, plants, and microorganisms.[1] It is a low molecularweight protein that exists as three different forms such as manganese SOD,copper–zinc SOD, and extracellular SOD.[1][2]
• Application: Superoxide Dismutase from bovine erythrocytes has been used in a study to assess activity parameters in adjuvant-induced arthritis. [3] Superoxide Dismutase from bovine erythrocytes has also been used in a study to simplify the process of purifying superoxide dismutases using charge-controlled hydrophobic chromatography on 10-carboxydecyl Sepharose. [4]It has also been used as a standard in SOD assay in mice liver andkidney samples.[5]
• Biochem/physiol Actions: Superoxide Dismutase from bovine erythrocytes catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. It serves as an antioxidant and plays a critical role in the defense of cells against the toxic effects of oxygen radicals. Competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice.
• Unit Definition: One unit will inhibit reduction of cytochrome c by 50% in a coupled system with xanthine oxidase at pH 7.8 at 25 °C in a 3.0 mL reaction volume. Xanthine oxidase concentration should produce an initial ΔA550 of 0.025 ± 0.005 per min.