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CAS:9054-89-1
Appearance:Blue green freeze-dried powder
Storage:Store at -20℃，2 years
Product introduction
SOD from bovine erythrocytes was the first SOD to be found in mammalian tissues. Before its
enzymatic activity was discovered the protein was known as haemocuprein or erythrocuprein.
Superoxide Dismutase (SOD) catalyzes the conversion of superoxide radicals into hydrogen peroxide
and molecular oxygen.
2 O2–+ 2 H+ → O2+ H2O
SOD from bovine erythrocytes is a homodimeric non-covalently bound protein with two 16.3kDa
subunits of 151 amino acids. Each monomer has one intrachain disulfide and one free sulfhydryl, one Cu2+
atom and one Zn2+ atom.
There are three forms of SOD differentiated by the metal ions in the active site. These are Cu2+/Zn2+
, Mn2+, and Fe2+ SOD. In vertebrate organisms Cu/Zn-SOD is found in the cytoplasm and the mitochondrial
intermembrane space, while Mn-SOD is found in the mitochondrial matrix space. Fe-SOD is found in prokaryotes and some higher plants.
Scope of application
It catalyzes the dismutation of superoxide radicals to form hydrogen peroxide and oxygen molecules. It plays an important role in cellular defense against the toxic effects of oxygen free radicals.
Usage method
SOD is soluble in water (20 mg/ml) yielding a colorless to blue-green solution. SOD is also soluble in aqueous buffers such as 0.1 M potassium phosphate, pH 7.5.
Isoelectric point
4.95
Optimum pH
7.8
pH Stability
7.6–10.5
Optimum temperature
25 ℃
Inhibitors
cyanide, OH–
(competitive), hydrogen peroxide
Matters needing attention
For Laboratory Use Only. Not for drug, household or other uses.
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