超氧物岐化酶提纯研究

Purification of Cu-Zn Superoxide Dismutase

采用氯仿—乙醇提取液盐析、丙酮沉淀及ＤＥ（３２）纤维素柱层析方法，从牛红细胞中分离得到纯品铜锌超氧物歧化酶（Ｃｕ、Ｚｎ—ＳＯＤ）．纯化的酶经聚丙烯酰胺凝胶电泳为一条蛋白带，活性染色在蛋白带的位置上呈现表示酶活性的亮斑，比活力为每毫克２４８７３单位，原子吸收测Ｃｕ、Ｚｎ含量及紫外吸收光谱测定结果制备样与标准ＳＯＤ样相同．

Cu-Zn Superoxide Dismutase was purified from bovin erythrocytes by treatment with mixtures of chloroform and ethanol, following precipitation withK2HPO4. acetone and chromotagraphy of DEAE- 32 column. The purified enzymeshowed one protein band by PAGE and was active at this protein band by activity dye.It's specific activity was 24873 unite per mg. It is indicated that the purified SOD is thesame as the standard SOD through ultraviolet absorption spectra and quantitation ofCopper and Zinc by atomic absorption spectrophotometry.