Abstract: Objective:To purify copper/zinc superoxide dismutase (Cu, Zn-SOD) from erythrocytes of chicken and to study some properties of purified Cu, Zn-SOD. Methods:Cu, Zn-SOD has been purified from erythrocytes of chicken by chloroform-ethanol fractionation, acetone precipitation, thermal denaturalization and DEAE-32 chromatography. Results:5.9 mg of dry powder enzyme was obtained, the purified specific activity of the enzyme was 10196.27 U/mg protein, the yield was 70.46%, and its purification time was 125.82. The investigation of physiochemical properties of the SOD showed that the ultraviolet absorption peak of the enzyme was found to be at 264 nm, which has two identical subunit, the molecular weight about 31000 D and the molecular weigh of subunit about 16500 D. The enzyme was found to have good stability at the pH range from 6 to 9 and good thermal stability at the 40 ℃ to 60 ℃ range over 30 mimutes incubation period. The Cu, Zn-SOD was not obviously inhibited by 2 mol/L SDS, but obviously inhibited by H2O2 and KCN. Conclusion:Cu, Zu-SOD is rich in the erythrocytes of chicken.

Key words: erythrocytes of chicken, copper and zinc superoxide dismutase, purification, property