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中华稻蝗谷胱甘肽S-转移酶的分离纯化
引用本文:郭艳琼,吴海花,宣涛,张建珍,郭亚平,马恩波.中华稻蝗谷胱甘肽S-转移酶的分离纯化[J].昆虫知识,2011,48(4):826-830.
作者姓名:郭艳琼  吴海花  宣涛  张建珍  郭亚平  马恩波
作者单位:1. 山西大学应用生物学研究所,太原,030006;山西农业大学农学院,太谷,030801
2. 山西大学应用生物学研究所,太原,030006
基金项目:国家自然科学基金重大国际合作项目,国家自然科学基金,中国博士后科学基金
摘    要:采用硫酸铵沉淀法和GSH-agarose亲和层析法,对中华稻蝗Oxya chinensis(Thunberg)5龄若虫谷胱甘肽S-转移酶(glutathione S-transferases,GSTs)进行了分离纯化.结果表明:经硫酸铵沉淀,饱和度在60%-80%下沉淀中GSTs比活力较高,饱和度90%时比活力达到最高...

关 键 词:谷胱甘肽硫转移酶  中华稻蝗  纯化  亲和层析

Affinity chromatography for the purification of glutathione S-transferase from Oxya chinensis
GUO Yan-Qiong,WU Hai-Hua,XUAN Tao,ZHANG Jian-Zhen,GUO Ya-Ping,MA En-Bo.Affinity chromatography for the purification of glutathione S-transferase from Oxya chinensis[J].Entomological Knowledge,2011,48(4):826-830.
Authors:GUO Yan-Qiong  WU Hai-Hua  XUAN Tao  ZHANG Jian-Zhen  GUO Ya-Ping  MA En-Bo
Institution:GUO Yan-Qiong 1,2 WU Hai-Hua1 XUAN Tao 1 ZHANG Jian-Zhen 1 GUO Ya-Ping 1 MA En-Bo 1 (1.Institute of Applied Biology,Shanxi University,Taiyuan 030006,China,2.College of Agriculture,Shanxi Agriculture University,Taigu 030801,China)
Abstract:Glutathione S-transferase (GST) in the fifth-instar nymphs of Oxya chinensis(Thunberg)was purified by ammonium sulfate and GSH-agrose affinity chromatography.Higher specific activity of GSTs could be detected at 60%-80% purity,and the highest specific activity was found at 90%.The specific activity was 0.3046 μmol/min/mg protein,and the purification factor was 1.82-fold.Further GSH-agrose affinity chromatography indicated that purification reached 50.88 with specific activity of 8.5185 μmol/min/mg protein.SDS-PAGE analysis indicated that the purified GSTs preparation had a single band with a relative molecular mass of 25.4 ku.These results provide the basis for further study of the enzymatic properties,structural characteristics and functions of the GSTs of O.chinensis.
Keywords:glutathione S-transferases (GSTs)  Oxya chinensis  purification  affinity chromatography  
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