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:

• for measuring mitochondrial hydrogen peroxide production in skeletal muscle
• as a positive control in Cu(II) binding stability assay
• as a positive control in superoxide dismutase assay
• in a study to assess the inactivation of endothelial-derived relaxing factor by oxidized lipoproteins.
• in a study to investigate the role of hydrogen peroxide in the cytotoxicity of the xanthine/xanthine oxidase system.

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 Signaling

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.

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.

Suspension in 3.8 M (NH₄)₂SO₄, pH 7.0