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新疆葡萄干超氧化物歧化酶的分离提纯

Separation and Purified of Xinjiang Raisin Superoside Dismutase

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【作者】 何俊李毓琦魏素萱白小清

【Author】 He Jun, Li Yuqi, Wei Shuxuan, Bai XiaoqingSchool of pharmacy, West China University of Medical Sciences (Chengdu 610041)

【机构】 华西医科大学药学院!成都610041

【摘要】 本文首次对新疆葡萄干中超氧化物歧化酶进行了分离提纯.酶活力测定采用微量邻苯三酚自氧化法.结果表明:100g新疆葡萄干经粗抽提,丙酮两步沉淀,Sephadex G-100柱层析,DEAE-52柱层析,得2.73mg酶蛋白,比活为408.8u/mg pro,纯化倍数为92.9,达电泳纯.

【Abstract】 Superoxide Dismutase (SOD) was separated and purified from Xinjiang raisin. Enzyme activity was determed with the autoxidation of pyrogallol method. The result shows that 100g Xinjiang raisin would be obtained 2. 73 mg enzyme protein by extraction, precipitation with actone, and sephadex G-100 colum chromatograph. This enzyme activity was 408. 80 u/mg. The puritic coefficient was 92. 9, electrophoretic purity.

  • 【文献出处】 中国生化药物杂志 ,Chinese Journal of Biochemical Pharmaceutics , 编辑部邮箱 ,1994年01期
  • 【分类号】R284
  • 【被引频次】9
  • 【下载频次】118
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