Oximes-induced reactivation of rat brain acetylcholinesterase inhibited by VX agent
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu srovnávací studie, časopisecké články, práce podpořená grantem
- MeSH
- acetylcholinesterasa metabolismus MeSH
- cholinesterasové inhibitory farmakologie MeSH
- krysa rodu Rattus MeSH
- mozek účinky léků enzymologie MeSH
- organothiofosforové sloučeniny farmakologie MeSH
- oximy chemie farmakologie MeSH
- potkani Wistar MeSH
- reaktivátory cholinesterázy chemie farmakologie MeSH
- techniky in vitro MeSH
- zvířata MeSH
- Check Tag
- krysa rodu Rattus MeSH
- mužské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- srovnávací studie MeSH
- Názvy látek
- acetylcholinesterasa MeSH
- cholinesterasové inhibitory MeSH
- organothiofosforové sloučeniny MeSH
- oximy MeSH
- reaktivátory cholinesterázy MeSH
- VX MeSH Prohlížeč
A comparison of one mono- and seven bisquaternary acetylcholinesterase (AChE) reactivators of acetylcholinesterase inhibited by VX agent was performed. As a source of the acetylcholinesterase, a rat brain homogenate was taken. There were significant differences in reactivation potency of all tested oximes. The oxime TO205 seems to be the most efficacious followed by TO046, HI-6, HS-6, K027, obidoxime, MMC and 2-PAM. In addition, the results of this study showed that the reactivation potency of the tested reactivators depends on many factors--such as the number of pyridinium rings, the number of oxime groups and their position, as well as the length and the shape of linkage bridge between two pyridinium rings.
Citace poskytuje Crossref.org
Reactivation of organophosphate-inhibited acetylcholinesterase by quaternary pyridinium aldoximes
