SOD | Superoxide Dismutase from porcine blood

Analysis consideration.
For the determination method, see McCord, J.M. And Fridovich, I., J. Biol. Chem., 244, 6049 (1969).

Biochemical / physiological behavior.
Catalyze the disproportionation of superoxide radicals to form hydrogen peroxide and oxygen molecules. It plays a key role in cell defense against the toxicity of oxygen free radicals. Compete with nitric oxide (NO) for superoxide anion (react with NO to form peroxynitrite), thus improve the activity of NO. SOD also showed an inhibitory effect on apoptosis in cultured rat follicles, nerve cell lines and transgenic mice.

General description.
Superoxide dismutase (SOD) is a group of low molecular weight metal proteins found in all aerobic cells of plants, animals and microorganisms. They prevent harmful reactions with superoxide anion radicals (O2 -) by catalyzing their disproportionation to oxygen and hydrogen peroxide.

Unit definition.
In the coupling system formed with xanthine oxidase, one unit in the 3.0mL reaction volume can inhibit the reduction of cytochrome c by 50% at pH 7.8C and 25 °C. The concentration of xanthine oxidase should produce an initial Δ A550 of 0.025 ±0.005 per minute.

Physical form.
Freeze-dried powder containing potassium phosphate buffer salt.

Application.
Superoxide dismutase has been used to determine that hypercholesterolemia increases endothelial superoxide anion production. Superoxide dismutase is also used to study diazo coupling, subunit interaction and electrophoretic variation of superoxide dismutase in erythrocytes.