铜离子螯合亲和层析纯化人铜锌超氧化物歧化酶

Purification of Cuprozinc Superoxide Dismu-tase From Human Erythrocytes by Cu￣(2+)Chelate Affinity Chromatography.

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．

uprozinc superoxide dismutase(CuZn-SOD)from human erythrocytes was purified by aprocedure involving Cu￣(2+) chelate affinity chro-matography.It was shown in three experi-ments that the special chromatography held anumber of important advantages for proteinpurification,such as a high rate of repeatingperformance and a large protein capacity. Thepurified enzyme,with a specific activity of3073 U/mg protein, was tested for homogene-ity by activity-stained and SDS gel elec-trophoresis.Accompanied by the study,a sim-ple and efficient method was worked out forassessing the homogeneity of CuZn-SOD usingits ratio of the absorbence at 260nm to that at280nm.