Superoxide Dismutase bovine

Research area: Cell Signaling

SOD from bovine erythrocytes was the first SOD to be found in mammalian tissues. There are three forms of SOD differentiated by the metal ions in the active site. These are Cu⁺²/Zn⁺², Mn⁺², and Fe⁺²SOD. In vertebrates, Cu/Zn-SOD is found in the cytoplasm, chloroplast, and may be in extracellular space, while Mn-SOD is found in the mitochondrial matrix space and peroxisome. Fe-SOD is found in the chloroplast of prokaryotes and some higher plants.

Superoxide Dismutase bovine has been used:

• to construct a calibration curve for the evaluation of superoxide dismutase (SOD) enzyme activities
• in a study to investigate where lipoproteins may affect the L-arginine-nitric oxide pathway
• in a study to investigate the mass spectral evidence for carbonate-anion-radical-induced posttranslational modification of tryptophan to kynurenine in human Cu, Zn superoxide dismutase

Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. This reaction in turn activates redox-sensitive kinases and inactivates specific phosphatases to regulate redox-sensitive signaling pathway, including hypertrophy, proliferation, and migration. SOD serves as a potent antioxidant and protects the cells against the toxic effects of oxygen radicals. SOD may also suppress apoptosis by competing with nitric oxide (NO) for superoxide anion, which reacts with NO to form peroxynitrite, an inducer of apoptosis.

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.

Produced using animal component-free materials.

Reconstitute in 10 mM potassium phosphate, pH 7.4.

Extinction coefficient: E^mM= 10.3 (258 nM)
SOD has no significant absorbance peak at 280 nM because of the absence of tryptophan.

Inhibitors: cyanide, OH^- (competitive), hydrogen peroxide