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Reactivation of immobilized acetylcholinesterase-tabun complex by pralidoxime, its isomers, and homologs
M. Hoskovcová, E. Halámek, Z. Kobliha, I. Tušarová
Language English Country England, Great Britain
Document type Journal Article
- MeSH
- Acetylcholinesterase drug effects MeSH
- Cholinesterase Inhibitors toxicity MeSH
- Isomerism MeSH
- Organophosphates toxicity MeSH
- Pralidoxime Compounds chemistry pharmacology MeSH
- Swine MeSH
- Cholinesterase Reactivators pharmacology MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
Reactivation efficacy of three homologous and three isomeric series of pralidoxime-type reactivators with aldoxime group in position 2, 3 and 4 of the heterocycle was tested in reactivation of tabun-inhibited AChE. The experiments were performed with immobilized and stabilized porcine brain AChE. The enzyme activity was measured by Ellman method. Reactivation efficacy was determined by measurement of indicator fabric coloration intensity as a measure of AChE activity. Of the studied group of nine reactivators, isomers with the functional group in position 2 were the most effective. The highest value (30 %) for reactivation of inhibited AChE was found for 2PAE after treatment for 15 min at concentration 0.5 mg/cm(3). The efficacy of the isomers decreased in the order ortho > para > meta. No marked effect on the efficacy of the reactivators was observed on prolongation of the reactivation time. The reactivators efficacy decreased with decreasing concentration of their solutions.
References provided by Crossref.org
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