Source: Porcine erythrocytes
Vitality: ≥2500u/mg protein
Introduction: The catalytic O2-+O2-+2H+=H2O2+O2 reaction contains two identical subunits. According to the different metal auxiliary ions, they are divided into three types: Cu-Zn-SOD, each subunit contains copper and zinc ions each with a molecular weight of 34000±(4%); Mn-SOD, with a molecular weight of 400,000; Fe-SOD, with a molecular weight of approximately 40000.
Superoxide dismutase (SOD) catalyzes the removal of the O2- free radical. The enzyme protects oxygen-metabolizing cells against harmful effects of superoxide free-radicals. Superoxide dismutase is inactivated by H2O2. It consists of two subunits of identical molecular weight joined by a disulfide bond. The molecular weight is 32,500 daltons, and there are two Cu(II) and two Zn(II) atoms per molecule. The isoelectric point of the enzyme is 4.95.