Notice of RetractionKinetic Studies for the Inhibition Effect of 4-Chlorophenol on Acetylcholinesterase Activity

2011 5th International Conference on Bioinformatics and Biomedical Engineering Pub Date : 2011-05-10 DOI:10.1109/ICBBE.2011.5781411

Q. Liu, Jun-xia Liu

引用次数: 0

Abstract

The inhibition effect of 4-chlorophenol (4-CP) on acetylcholinesterase (AChE) and its kinetics were studied by spectrophotometry. The results show that the activity of AChE can be inhibited obviously by 4-CP, and the 50% inhibitory concentration (IC₅₀) is 0.66 mmol·L^-1. 4-CP acted as a mixed inhibitor of AChE, and a reversible inhibition mechanism were observed. Lineweaver-Burk plot results showed that the mixed inhibitory constants K_i and K'_i were 0.55 mmol·L^-1 and 1.60 mmol·L^-1, respectively, which indicated that the inhibition effect of 4-CP on free enzyme was stronger than that on enzyme-substrate complex.

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4-氯酚抑制乙酰胆碱酯酶活性的动力学研究

采用分光光度法研究了4-氯酚(4-CP)对乙酰胆碱酯酶(AChE)的抑制作用及其动力学。结果表明，4-CP能明显抑制乙酰胆碱酯酶活性，50%抑制浓度(IC50)为0.66 mmol·L-1。4-CP作为AChE的混合抑制剂，并观察到可逆抑制机制。Lineweaver-Burk图结果显示，4-CP对游离酶的抑制作用强于对酶-底物复合物的抑制作用，其混合抑制常数Ki和K'i分别为0.55 mmol·L-1和1.60 mmol·L-1。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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2011 5th International Conference on Bioinformatics and Biomedical Engineering

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