【摘要】 采用热变性─硫酸铵分级沉淀─Ｓｅｐｈａｄｅｘ Ｇ－１００和 ＤＥ ５２柱层析 的方法从贻贝中分离纯化铜锌超氧化物歧化酶（Ｃｕ、Ｚｎ－ＳＯＤ），并对其部分性质进行 分析鉴定。结果该酶的比活力为 ９ ４５３． ３ Ｕ／ｍｇ（ｐｒｏｔｅｉｎ），提纯倍数为 ６０９． ９；对ＫＣＮ 和 Ｈ_２Ｏ_２敏感，Ｔ氏液和 ＳＤＳ对酶活性没影响；对热较稳定。紫外吸收峰在 ２７０ ｎｍ 处，聚丙烯酰胺凝胶电泳呈现３条谱带，亚基分子量为１６ ５００ｕ。更多还原

【Abstract】 A method of heating denaturation, precipitation with ammonium sulphate and passing Sephadex G-100 and DE 52 chromatography colums was used to separate and purify superox ide dismutase containing copper and zinc（Cu,Zn-SOD） from Mytilus,and part of its charac ters were analyzed. The results showed that the specific activity of the enzyme was 9 453. 3 U/mg, and its multiple purified was 609. 9. The enzyme was sensitive to KCN and H₂O₂,and not sensitive to Tsuchihashi solution and SDS. It was stable in heat condition. Its ultraviolet absorption maxinum was at 270 nm. It showed three bands by polyacrylamide gel elec trophoresis. The enzymy subunit molecular weight was 16 500u.更多还原