毛蚶超氧化物歧化酶的纯化、部分性质与修饰

经热变性 硫酸铵分级沉淀，微量铜离子溶液秀析，Sephadex G-100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)，并对其是化性质进行分析鉴定，实验结果获得该 比活力为5294．1U／mg，提纯倍数为885．9，该酶对KCNM和H2O2敏感，而suchihashi液对酶活性没影响，对热较稳定，紫外吸收峰城260nm处，聚丙烯酰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28．8kD，每个亚其含有一原子铜和一原子锌，经右旋糖甙修饰后抗胃蛋白酶水解的能力增强。

Purification, characterization and modification of superoxide dismustase from Arca subcrenata lischke

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.