Superoxide Dismutase from bovine liver

For assay method, see McCord, J.M. and Fridovich, I., J. Biol. Chem., 244, 6049 (1969).

Superoxide dismutase from bovine liver has been used in a study to determine that hypercholesterolemia increases endothelial superoxide anion production. Superoxide dismutase from bovine liver has also been used in a study to investigate diazo coupling, subunit interactions, and electrophoretic variants of bovine erythrocyte superoxide dismutase. It has also been used as a component of the assay buffer in thequantification of reactive oxygen species (ROS) by O2k fluorometry.

Superoxide Dismutase catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. It plays a critical role in the defense of cells against the toxic effects of oxygen radicals. It 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.

Research area: Cell signalingSuperoxide Dismutase (SOD), a low molecular weight protein that is found in all aerobic cells of microorganisms, plants, and animals. It exists as three distinct families such as manganese SOD, copper–zinc SOD, and extracellular SOD.

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.

Lyophilized powder containing potassium phosphate buffer salts