Pohanka_2015_J.Enzyme.Inhib.Med.Chem_30_796

Reference

Title : Evaluation of 2,6-dichlorophenolindophenol acetate as a substrate for acetylcholinesterase activity assay - Pohanka_2015_J.Enzyme.Inhib.Med.Chem_30_796
Author(s) : Pohanka M , Holas O
Ref : J Enzyme Inhib Med Chem , 30 :796 , 2015
Abstract :

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 microM 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.

PubMedSearch : Pohanka_2015_J.Enzyme.Inhib.Med.Chem_30_796
PubMedID: 25672529

Related information

Citations formats

Pohanka M, Holas O (2015)
Evaluation of 2,6-dichlorophenolindophenol acetate as a substrate for acetylcholinesterase activity assay
J Enzyme Inhib Med Chem 30 :796

Pohanka M, Holas O (2015)
J Enzyme Inhib Med Chem 30 :796