Efficacy of structural homoloques and isomers of pralidoxime in reactivation of immobilised acetylcholinesterase inhibited with sarin, cyclosarin and soman
Jazyk angličtina Země Švédsko Médium print
Typ dokumentu časopisecké články
PubMed
20027163
PII: NEL300709A26
Knihovny.cz E-zdroje
- MeSH
- acetylcholinesterasa metabolismus MeSH
- biosenzitivní techniky MeSH
- cholinesterasové inhibitory chemie toxicita MeSH
- enzymy imobilizované antagonisté a inhibitory metabolismus MeSH
- isomerie MeSH
- organofosforové sloučeniny chemie farmakologie MeSH
- oximy chemie farmakologie MeSH
- pralidoximové sloučeniny chemie farmakologie MeSH
- reaktivátory cholinesterázy chemie farmakologie MeSH
- sarin toxicita MeSH
- soman toxicita MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- acetylcholinesterasa MeSH
- cholinesterasové inhibitory MeSH
- cyclohexyl methylphosphonofluoridate MeSH Prohlížeč
- enzymy imobilizované MeSH
- organofosforové sloučeniny MeSH
- oximy MeSH
- pralidoxime MeSH Prohlížeč
- pralidoximové sloučeniny MeSH
- reaktivátory cholinesterázy 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.