Purification of Acetylcholinesterase from Locusta migratoria and preliminary study on pesticide screening
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S482.3

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    Abstract:

    AChE was purified by affinity chromatography from Locusta migratoria head. The purification factors and yields were 474.81fold and 28.93%, respectively. The molecular weight of the purified enzyme was 67.22kDa, measured by SDSPAGE. The inhibitory activity of 24 furanone analogs against AChE and the toxic effect against RPHzVNCAW1(AW1)were measured, then the relevance of cytotoxicity and inhibitory effects was discussed. The results showed that 19 compounds had inhibitory effects on AChE and 13 compounds with cytotoxicity on AW1 cells. Compound Ⅱ had shown better relevance to AChE activity with cytotoxicity . The AChE inhibition rate of Ⅱ3 was (80.94 + 3.09)% under the concentration of 100 mg/L and cytotoxicity activities was (95.01±2.24) % under the concentration of 50 mg/L.

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Cite this article as: DENG Yuan-Jie, ZHANG Xiao-Xiao, GAO Tian-Tian, TAO Ke, JIN Hong, HOU Tai-Ping. Purification of Acetylcholinesterase from Locusta migratoria and preliminary study on pesticide screening [J]. J Sichuan Univ: Nat Sci Ed, 2018, 55: 637.

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History
  • Received:April 07,2017
  • Revised:May 18,2017
  • Adopted:May 20,2017
  • Online: June 06,2018
  • Published: