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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.
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 , 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.