【摘要】 经热变性 ,硫酸铵分级沉淀 ,微量铜离子溶液透析 ,Sephadex G- 10 0凝胶过滤和 DE- 52柱层析 ,从毛蚶中分离纯化铜锌超氧化物歧化酶 (Cu,Zn- SOD) ,并对其部分理化性质进行分析鉴定。实验结果获得该酶的比活力为 52 94 .1U/ mg,提纯倍数为 885.9,该酶对 KCN和 H2 O2 敏感 ,而 Tsuchihashi液对酶活性没影响 ,对热较稳定 ;紫外吸收峰在 2 6 0 nm处 ;聚丙烯酰胺凝胶电泳蛋白带与活性带相对应 ;该酶是由 2个相同亚基组成的二聚体 ,分子量为 2 8.8k D;每个亚基含有一原子铜和一原子锌。经右旋糖苷修饰后抗胃蛋白酶水解的能力增强更多还原

【Abstract】 Copper Zinc Superoxide Dismustase was purified from Arca subcrenata Lischke by heating denaturation, precipitation with ammonium sulfate dialysis in the presence of Cu 2+ , Sephadex G 100 filtration and DE 52 chromatography. And parts of its characters were analyzed. The results showed that the specific activity of the enzyme was 5294.1 U/mg, and its purification factor was 886. The enzyme was sensitive to KCN and H 2O 2, but it was not sensitive to Tsuchihashi solution. The enzyme was stable in heat condition. And the ultraviolet absorption peak of the enzyme was found at 260nm. The enzyme was showed that its protein bands correspond with its activity bands by polyacrylamide gel eletrophoresis. The enzyme was composed of two equally sized subunits. Its molecular weight was 28.8kD. Every subunit contains one copper atom and one zinc aton. The modified enzyme by dextran had antagonism with pepsin.更多还原