Evaluation of 2, 6-dichlorophenolindophenol acetate as a substrate for acetylcholinesterase activity assay. (October 2015)

• Record Type: Journal Article
• Authors: Pohanka, Miroslav; Holas, Ondrej
• Is Part Of: Journal of enzyme inhibition and medicinal chemistry. Volume 30:Number 5(2015:Oct.)
• Page Start: 796
• Page End: 799
• Publication Date: 2015-10
• Subjects: Enzyme inhibitors -- Periodicals; Enzyme Inhibitors -- periodicals; Biochemistry -- periodicals; 572.7
• Languages: English
• ISSNs: 1475-6366

Abstract

<abstract> <title>Abstract</title> <p>Ellman's method is a standard protocol for the determination of cholinesterases activity. Though the method is ready for laboratory purposes, it has some drawbacks as well. In the current article, 2, 6-dichloroindophenol acetate is performed as a chromogenic substrate suitable for acetylcholinesterase (AChE) activity examination. Michaelis constant and maximal velocity for 2, 6-dichloroindophenol acetate were determined (38.0 µM and 244 pkat) and compared to the values for acetythiocholine (K_m 0.18 mM; V_max 5.1 nkat). Docking for 2, 6-dichloroindophenol acetate and human AChE was done as well. In conclusion, 2, 6-dichloroindophenol acetate seems to be suitable chromogenic substrate for AChE and spectrophotometry and based on this it can be easily performed whenever AChE activity should be tested.</p> </abstract>