Oximes-induced reactivation of rat brain acetylcholinesterase inhibited by VX agent
Language English Country England, Great Britain Media print
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Acetylcholinesterase metabolism MeSH
- Cholinesterase Inhibitors pharmacology MeSH
- Rats MeSH
- Brain drug effects enzymology MeSH
- Organothiophosphorus Compounds pharmacology MeSH
- Oximes chemistry pharmacology MeSH
- Rats, Wistar MeSH
- Cholinesterase Reactivators chemistry pharmacology MeSH
- In Vitro Techniques MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Male MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Acetylcholinesterase MeSH
- Cholinesterase Inhibitors MeSH
- Organothiophosphorus Compounds MeSH
- Oximes MeSH
- Cholinesterase Reactivators MeSH
- VX MeSH Browser
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.
References provided by Crossref.org
Reactivation of organophosphate-inhibited acetylcholinesterase by quaternary pyridinium aldoximes
