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In vitro potency of H oximes (HI-6, HLö-7), the oxime BI-6, and currently used oximes (pralidoxime, obidoxime, trimedoxime) to reactivate nerve agent-inhibited rat brain acetylcholinesterase
Kuca K, Cabal J, Kassa J, Jun D, Hrabinova M.
Journal of toxicology and environmental health. Part A.
2006 ;
69 (15) :
1431-1440.
Jazyk angličtina Země Velká Británie
Perzistentní odkaz
https://www.medvik.cz/link/bmc07522305
- MeSH
- acetylcholinesterasa fyziologie MeSH
- antidota farmakologie MeSH
- chemické bojové látky farmakologie MeSH
- cholinesterasové inhibitory farmakologie MeSH
- financování organizované MeSH
- krysa rodu rattus MeSH
- mozek účinky léků MeSH
- obidoxim chlorid farmakologie MeSH
- organofosfáty farmakologie MeSH
- organothiofosforové sloučeniny farmakologie MeSH
- oximy farmakologie MeSH
- potkani Wistar MeSH
- pralidoximové sloučeniny farmakologie MeSH
- pyridinové sloučeniny farmakologie MeSH
- pyridiny farmakologie MeSH
- reaktivátory cholinesterázy farmakologie MeSH
- trimedoxim farmakologie MeSH
- zvířata MeSH
- Check Tag
- krysa rodu rattus MeSH
- mužské pohlaví MeSH
- zvířata MeSH
The efficacy of H oximes (HI-6, HLö-7), the oxime BI-6, and currently used oximes (pralidoxime, obidoxime, trimedoxime) to reactivate acetylcholinesterase inhibited by two nerve agents (tabun, VX agent) was tested in vitro. Both H oximes (HI-6, HLö-7) and the oxime BI-6 were found to be more efficacious reactivators of VX-inhibited acetylcholinesterase than pralidoxime and obidoxime. On the other hand, their potency to reactivate tabun-inhibited acetylcholinesterase was low and did not reach the reactivating efficacy of trimedoxime and obidoxime. Thus, none of these compounds can be considered to be a broad-spectrum reactivator of nerve agent-inhibited acetylcholinesterase in spite of high potency to reactivate acetylcholinesterase inhibited by some nerve agents. More than one oxime may be necessary for the antidotal treatment of nerve agent-exposed individuals.
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