@article{APS4944,
author = {Yi Luo and Song-Cheng Yang and Qi-Kai Zhang},
title = {Action of VX on torpedo acetylcholinesterase},
journal = {Acta Pharmacologica Sinica},
volume = {8},
number = {1},
year = {2016},
keywords = {},
abstract = {The action of VX (O-ethyl-S-(2-diisopropylaminoethyl) methylphosphonothiolate) on torpedo acetylcholinesterase was studied by means of capillary column GC, GC-MS and [35S] VX. The immobilized torpedo AChE nylon net was used. The results showed that VX inhibited the enzyme not only by phosphorylation but also by forming dithio-complex compound with the mercapto group in the active center of the AChE. Under physiological condition, 92% VX presents as its protonated form and 8% as free base, the cationic part of VX protonated form is coulombically bound to anionic site of the enzyme selectively.},
issn = {1745-7254}, url = {http://www.chinaphar.com/article/view/4944}
}