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大豆超氧化物歧化酶的分离和鉴定
Isolation and Characterization of Superoxide Dismutase from Soybean
【摘要】 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。
【Abstract】 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.
- 【文献出处】 中国生化药物杂志 ,Chinese Journal of Biochemical Pharmaceutics , 编辑部邮箱 ,1996年02期
- 【分类号】Q55
- 【被引频次】12
- 【下载频次】198