大豆超氧化物歧化酶的分离和鉴定

Isolation and Characterization of Superoxide Dismutase from Soybean

采用磷酸盐缓冲液使样品匀浆,两次硫酸铵分级沉淀和DEAE-Cellulose离子交换层析从大豆中分离出超氧化物歧化酶。分离酶的聚丙烯酰胺凝胶电泳呈一条蛋白谱带。过氧化氢和乙醇-氯仿试验表明,该酶属铜锌超氧化物歧化酶。酶的比活力为4710u/mg Pr,活力回收率23％,紫外吸收峰在265.4nm,分子量为32.4kD。

This paper reported the isolation and purification of superoxide dismutase from soybean by homogenating with pH 7. 8 PBS, ammonium sulfate fractionation and DEAE-Cellulose ion exchange chromatography. The purified enzyme was showed a single band on -PAGE. Through treatment with H2O2 or ethanolchloroform, the results indicated the enzyme being Cu, Zn-SOD. Its specific activity is estimated as 4 710 u/mg protein, the yield of activity being 23%, maxinum ultraviolet absorption spectrum 265. 4 nm and molecular weight 32 400 dalton.