期刊
BIOSENSORS & BIOELECTRONICS
卷 24, 期 7, 页码 2119-2124出版社
ELSEVIER ADVANCED TECHNOLOGY
DOI: 10.1016/j.bios.2008.11.006
关键词
Acetylcholinesterase; Aflatoxin B1; Enzyme; Inhibition; Biosensor; Peripheral site
类别
资金
- CEA
- CNRS
- UJF
- Agence Nationale de la Recherche [JC05-45685]
In this paper, the inhibition effect of aflatoxin B1 on different species of cholinesterases was investigated to unravel action mechanism. The inhibition curves of several cholinesterase mutants (obtained by spectrophotometric measurements of enzyme activity, pS curves) were analyzed. They showed that this toxin reversibly inhibits cholinesterases by binding to a peripheral site located at the entrance of the active site gorge without entering inside the site. Electric eel enzyme revealed the highest inhibition extent with a binding constant estimated to 0.35 mu M. This binding prevents the entrance of substrate en route to the catalytic site and also decreases chemical steps of the reaction at the catalytic site: acetylation is reduced to the half and deacetylation is reduced to the third. Electric eel acetylcholinesterase was used to settle an amperometric biosensor. The best detection was obtained by using 0.3 mU enzyme on the electrode and 0.5 mM ATCh in the solution. The limit of detection was 3 mu M corresponding to 20% inhibition. (C) 2008 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据