Efficacy of structural homoloques and isomers of pralidoxime in reactivation of immobilised acetylcholinesterase inhibited with sarin, cyclosarin and soman
Language English Country Sweden Media print
Document type Journal Article
PubMed
20027163
PII: NEL300709A26
Knihovny.cz E-resources
- MeSH
- Acetylcholinesterase metabolism MeSH
- Biosensing Techniques MeSH
- Cholinesterase Inhibitors chemistry toxicity MeSH
- Enzymes, Immobilized antagonists & inhibitors metabolism MeSH
- Isomerism MeSH
- Organophosphorus Compounds chemistry pharmacology MeSH
- Oximes chemistry pharmacology MeSH
- Pralidoxime Compounds chemistry pharmacology MeSH
- Cholinesterase Reactivators chemistry pharmacology MeSH
- Sarin toxicity MeSH
- Soman toxicity MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Acetylcholinesterase MeSH
- Cholinesterase Inhibitors MeSH
- cyclohexyl methylphosphonofluoridate MeSH Browser
- Enzymes, Immobilized MeSH
- Organophosphorus Compounds MeSH
- Oximes MeSH
- pralidoxime MeSH Browser
- Pralidoxime Compounds MeSH
- Cholinesterase Reactivators MeSH
- Sarin MeSH
- Soman MeSH
OBJECTIVES: Quantification of efficacy of monopyridinium isomers and homologs derived from clinically used Pralidoxime within reactivation of acetylcholinesterase inhibited with organophosphorus nerve agents. METHODS: This work uses the colorimetric biosensor called Detehit - cotton cloth with immobilized enzyme acetylcholinesterase. Biosensor is based on the modificated Ellman's method. RESULTS: The highest reactivation was observed with sarin-inhibited acetylcholinesterase. Substantially lower reactivation was found with the cyclosarin-inhibited enzyme whereas AChE, inhibited by soman could not be effectively reactivated under the given conditions (enzyme inhibition for 2 minutes and subsequent treatment with the reactivator for 15 minutes). CONCLUSION: Our work gives comparison of efficacy of reactivators in dependence on the length of alkylene chain and position of aldoxime functional group. Evaluation of effectivity of aldoxime reactivators is provided by simple means. The method allows rapid in vitro evaluation of the reactivators without being disturbed by excess of the organophosphate or reactivator.
