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Tabun-inhibited rat tissue and blood cholinesterases and their reactivation with the combination of trimedoxime and HI-6 in vivo
J. Bajgar, JZ. Karasova, J. Kassa, J. Cabal, J. Fusek, V. Blaha, S. Tesarova,
Jazyk angličtina Země Irsko
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- acetylcholinesterasa krev metabolismus MeSH
- aktivace enzymů účinky léků MeSH
- centrální nervový systém účinky léků enzymologie metabolismus MeSH
- kombinovaná farmakoterapie MeSH
- krysa rodu rattus MeSH
- organofosfáty MeSH
- otrava organofosfáty MeSH
- oximy aplikace a dávkování farmakologie MeSH
- potkani Wistar MeSH
- pyridinové sloučeniny aplikace a dávkování farmakologie MeSH
- reaktivátory cholinesterasy aplikace a dávkování farmakologie MeSH
- trimedoxim aplikace a dávkování farmakologie MeSH
- zvířata MeSH
- Check Tag
- krysa rodu rattus MeSH
- ženské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Up to now, intensive attempts to synthesize a universal reactivator able to reactivate cholinesterases inhibited by all types of nerve agents/organophosphates were not successful. Therefore, another approach using a combination of two reactivators differently reactivating enzyme was used: in rats poisoned with tabun and treated with combination of atropine (fixed dose) and different doses of trimedoxime and HI-6, changes of acetylcholinesterase activities (blood, diaphragm and different parts of the brain) were studied. An increase of AChE activity was observed following trimedoxime treatment depending on its dose; HI-6 had very low effect. Combination of both oximes showed potentiation of their reactivation efficacy; this potentiation was expressed for peripheral AChE (blood, diaphragm) and some parts of the brain (pontomedullar area, frontal cortex); AChE in the basal ganglia was relatively resistant. These observations suggest that the action of combination of oximes in vivo is different from that observed in vitro.
Citace poskytuje Crossref.org
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