食品科学 ›› 2005, Vol. 26 ›› Issue (4): 91-94.

• 基础研究 • 上一篇    下一篇

鸭血浆胆碱酯酶的分离纯化和性质的研究

 刘畅, 陈福生, 李书谦, 路磊, 邢淑婕   

  1. 华中农业大学食品科技学院; 湖北省农业科学院
  • 出版日期:2005-04-15 发布日期:2011-09-19

Purification of Cholinesterase from Duck Serum

 LIU  Chang, CHEN  Fu-Sheng, LI  Shu-Qian, LU  Lei, XING  Shu-Jie   

  1. 1.College of Food Science and Technology, Huazhong Agriculture University; 2.Hubei Academy of Agricultural Sciences
  • Online:2005-04-15 Published:2011-09-19

摘要: 将鸭血浆用0.2mol/L pH7.2磷酸盐缓冲溶液等体积稀释后,以硫酸铵为盐析剂进行二次盐析、再经DEAE-52离子交换层析和Sephadex G-200凝胶过滤层析对胆碱酯酶进行分离纯化,可获得电泳纯的胆碱酯酶,纯化倍数为278.5倍,酶活回收为17.8%。实验表明,该酶的最适温度为37℃,最适pH为7.8,有过量底物抑制现象。

关键词: 胆碱酯酶, 鸭血浆, 盐析, 离子交换层析, 凝胶过滤层析

Abstract: Cholinesterase from duck serum was purified to electrophoretic homogeneity by salting out twice with ion-exchange chromatography on DEAE-cellulose and gel filtration on Sephadex G-200. The enzyme was purified 278.5-fold and the activity recovery 17.8% percent was obtained. Studies on the properties of the Cholinesterase showed that the optimum temperature was 37℃ and the optimum pH was between 7.5~8.0. The enzyme would be inhibited by excess butyryl-thiocholine iodide.

Key words: Cholinesterase, duck serum, salt out, ion-exchang chromatography, gel filtration