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 assess the inactivation of endothelial derived relaxing factor by oxidized lipoproteins. Superoxide dismutase from bovine liver has also been used in a study to investigate the role of hydrogen peroxide in the cytotoxicity of the xanthine/xanthine oxidase system.
Superoxide Dismutase from bovine liver has been used:for measuring mitochondrial hydrogen peroxide production in skeletal muscleas a positive control in Cu(II) binding stability assayas a positive control in superoxide dismutase assay
Catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. 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.
Superoxide dismutases are a group of low molecular weight metalloproteins present in all aerobic cells of plants, animals and micro-organisms. They provide protection against damaging reactions with the superoxide radical anion (O2-) by catalyzing its disproportionation into oxygen and hydrogen peroxide.
3000, 15000 units in glass bottle
Suspension in 3.8 M (NH4)2SO4, pH 7.0
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.
This product has met the following criteria: