【摘要】 经加热和硫酸铵分级沉淀、DE 52柱层析和SephadexG 1 0 0凝胶过滤 ,从缢蛏中分离纯化铜锌超氧化物歧化酶 (Cu ,Zn SOD) ,并对其理化性质进行分析鉴定 .结果获得该酶的比活力为 3 794.9(U/mg) ,提纯倍数为 60 7.7.聚丙烯酰胺凝胶电泳蛋白带与活性带相对应 ,等电点为 5.8.该酶是由两个相同的亚基组成的二聚体 ,相对分子质量为 2 9.6kD .紫外吸收峰在 2 75nm处 .KCN和H2 O2 能抑制酶活性 ,而Tsuchi hashi液对酶活性没影响 .该酶的最适 pH为 6～ 1 0 ,最适温度为 3 7℃ ,热稳定性在63℃以下 .更多还原

【Abstract】 Copper zinc superoxide dismustase was isolaled and purified from Sinonovacula constricta by heat treatment, precipitation with ammonium sulfate, DE 52 chromatography and Sephadex G 100 filtration. And its characters were analyzed. The results showed that the specific activity of the enzyme was 3 794.9 U/mg, and its purification factor was 607.7. The enzyme protein bands correspond with its actiyity bands by polyacrylamide gel eletrophoresis. Its pI was 5.8. The enzyme was composed of two equally size subunits. Its relative molecular quality was 29.6 kD. And the ultraviolet absorption peak of the enzyme was found at 275 nm. The enzyme was sensitive to KCN and H 2O 2 ,but it is not sensitive to Tsuchihashi solution. The enzyme optimum pH was from 6 to 10. And its optimum temperture was at 37℃ .The enzyme was stable below 63℃.更多还原