Abstract: Superoxide dismutases(SODs) were purified to homogeneity from Allium Sativum by means of ammonium sulfate precipitation and column chromatography with DEAE-cellulose(DE52) and Sephadex G-75. Based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-AGE), Allium Sativum is predicted to contain four SODs. The molecular weights of the native SODs are 41.3 kD, 37.0 kD, 35.2 kD and 31.0 kD, which consist of subunits of 20.7 kD, 18.4 kD, 17.7 kD and 15.4 kD respectively. Because of their specific sensitivity to hydrogen peroxide, cyanogens potassium and chloroform-alcohol, the SODs in Allium Sativum appear to be Cu, Zn-SOD isoenzymes. The isoelectric analysis indicates that three of the four isoenzymes are acidic proteins with isoelectric points at pH 3.5, 3.7 and 4.0, respectively, and the fourth one is a basic protein with isoeletric point at pH 8.5.

Key words: Superoxide dismutase, Allium Sativum, Purification, Properties