Reactivation of Human Acetylcholinesterase and Butyrylcholinesterase Inhibited by Leptophos-Oxon with Different Oxime Reactivators in Vitro

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00179906%3A_____%2F10%3A10082273" target="_blank" >RIV/00179906:_____/10:10082273 - isvavai.cz</a>
Alternative codes found
RIV/60460709:41330/10:49586 RIV/60162694:G44__/10:00002372
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Reactivation of Human Acetylcholinesterase and Butyrylcholinesterase Inhibited by Leptophos-Oxon with Different Oxime Reactivators in Vitro
Original language description
We have evaluated in vitro the potency of 23 oximes to reactivate human erythrocyte acetylcholinesterase (AChE) and plasma butyrylcholinesterase (BChE) inhibited by racemic leptophos-oxon (O-[4-bromo-2,5-dichlorophenyl]-O-methyl phenylphosphonate), a toxic metabolite of the pesticide leptophos. Compounds were assayed in concentrations of 10 and 100 mu M. In case of leptophos-oxon inhibited AChE, the best reactivation potency was achieved with methoxime, trimedoxime, obidoxime and oxime K027. The most potent reactivators of inhibited BChE were K033, obidoxime, K117, bis-3-PA, K075, K074 and K127. The reactivation efficacy of tested oximes was lower in case of leptophos-oxon inhibited BChE.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
FP - Other medical fields
OECD FORD branch
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Project
<a href="/en/project/IAA603020901" target="_blank" >IAA603020901: Actinomycete and fungi contribution to the decomposition of plant litter in the ecosystems contaminated with heavy metals.</a><br>
Continuities
V - Vyzkumna aktivita podporovana z jinych verejnych zdroju

Publication year
2010
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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