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《Journal of Sichuan University(Natural Science Edition)》 2008-01
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Purification and characterization of acetylcholinesterase,a kind of pesticide target

PENG Xia,TAO Ke,TENG Yun,HUANG Xiao,HOU Tai-Ping(Key Laboratory of Bio-resources and Eco-environment of Ministry of Education,College of Life Sciences,Sichuan University,Chengdu 610064,China)  
Acetylcholinesterase(AChE) of Bombyx mori Linaeus,separated from the crude extract,was purified to electrophoretic homogeneity by Sephadex G-25 chromatography,DEAE-Sepharose Fast Flow ion-exchange chromatography and Sephacryl S-200 gel filtration,respectively.The Molecular weight of the purified enzyme was 77.8 kDa,measured by SDS-PAGE.The optimum temperature of the AChE was 37 ℃,above which the enzyme would be unstable.It exhibited optimum activity at pH 7.5.The Michaelis constant for acetylthiocholine iodide was 0.392 mmol/L.The optimum concentration of substrate was 1.6 mmol/L,and the enzyme could be inhibitied by high level of acetylthiocholine iodide.
【Fund】: 国家自然科学基金(20572076);; 教育部博士点基金(20050610016)
【CateGory Index】: TQ450
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