摘要
用硫酸铵分级沉淀、葡萄糖凝胶过滤及离子交换柱层析从玉米中分离纯化SOD,并采用考马斯亮蓝G-250法测蛋白含量,NBT光还原法测定SOD酶活性,得到酶比活力为115.522U/mg.Pr,回收率为1.02%,提纯倍数7.77的SOD.同时进行了蛋白染色、SOD酶活性染色及非变性凝胶电泳(PAGE)研究,得到了电泳均一的SOD酶.
Superoxide dismutase （Cu, Zn-SOD）fmm maize was purified by a combination of ammonium sulfate fraetionation, Sephadex G-75 gel filtration and DEAE-32 chromatography. The purified enzyme was a highly homogeneous protein with the specific activity of 155.522 U/mg·pr. The yield rate is about 1.02%, and the multiplication is as high as 7.77 times. The bands of enzyme correspond with its activity bands bynondenaturing polyacrylamidegd electmphoresis. The results showed that the enzyme was a manganese superoxide.
出处
《沈阳师范大学学报（自然科学版）》
CAS
2006年第2期231-233,共3页
Journal of Shenyang Normal University:Natural Science Edition
关键词
超氧化物歧化酶
玉米
分离纯化
电泳
Superoxide dismutase
Maize
Extracting and purifying
Electrophoresis
