大蒜超氧化物歧化酶的分离纯化及其性质的研究  

Purification and Characterization of Superoxide Dismutase from Garlic

作　　者：王雪峰[1] 沈颂东[1] 迮玉官[1] 杨龙寿[2] 陈天[2] 张锦云[2] 

机构地区：[1]苏州大学生物科学系,江苏苏州215151 [2]扬州大学化学化工学院

出　　处：《安徽农业科学》2001年第3期408-409,共2页Journal of Anhui Agricultural Sciences

摘　　要：以壳聚糖为基质的金属螯合亲和层析法纯化大蒜SOD ,得到比活为 1191U/mg的酶蛋白 ,回收率为 71% ,纯化倍数为7.2 9。实验表明 ,经 8mol/L的尿素处理后大蒜SOD活性不发生变化 ,并且可耐 6 0℃高温Superoxide Dismutase(SOD) from garlic was purified with the metal chelate affinity chromatography(MCAC), using chitosan as substrate. The SOD was purified to homogeneous in one step affinity chromatography. Its specific activity was 1191U/mg and recover was 71%. The experiment demonstrated that SOD could resist the high temperature over 60℃for 1h.

关 键 词：大蒜 超氧化物歧化酶 金属螯合亲和层析 分离 纯化 酶学性质 

分 类 号：Q554.9[生物学—生物化学] Q949.718.2