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用铜离子螯合亲和层析对人红细胞铜锌超氧化物歧化酶进行了纯化．３次实验的结果表明，此项层析具有重复使用率高和蛋白结合量大的显著优点．提纯的人铜锌超氧化物歧化酶的比活性为３０３７Ｕ每毫克蛋白，并经活性染色和ＳＤＳ聚丙烯酰胺凝胶电泳证实其纯度均一．纯化中，探索了用紫外２６０ｎｍ与２８０ｎｍ的Ａ比值判断酶纯度的简便方法．
Human erythrocyte copper-zinc superoxide dismutase was purified using chelating affinity chromatography with copper ions. The results of three experiments showed that this chromatogram has the significant advantage of high reusability and large amount of protein binding. Purified human copper zinc superoxide dismutase specific activity of 3037U per mg protein, and confirmed by the activity of SDS polyacrylamide gel electrophoresis and purity uniformity. In the purification, a simple and convenient method to judge the purity of the enzyme by using the UV ratio of 260 nm and 280 nm was explored.