Action of VX on torpedo acetylcholinesterase
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.
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