RESUMEN
Superoxide dlsmutase [SOD] functions as a scavenger of superoxide radical, thus, it protects living organisms. Here we present a simple and efficient SOD purification method from human umbilical cord blood. After chloroform-ethanol treatment, SOD was purified by DEAE sepharose, phenyl-sepharose and HPLC. The purified enzyme has a molecular weight of 150,000 as determined by gel filtration and it appears as a single homogenous band on SDS-PAGE under non reducing and reducing conditions with an apparent molecular weight of 25,000, an indication that the native enzyme is a hexamer. It has a specific activity of 27x10[4] U/ mg protein. The optimum pH is 7.8 with a pi of 6.0 and the optimum temperature is 37.5°C. The enzyme has a Km of 2.7x10[4] and the activity is completely inhibited by 5 mM EDTA, while Cu and Zn regain and enhace the activity when added after EDTA inhibition. This means that this is a Zn-Cu SOD