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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,
Language English Country Ireland
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Acetylcholinesterase blood metabolism MeSH
- Enzyme Activation drug effects MeSH
- Central Nervous System drug effects enzymology metabolism MeSH
- Drug Therapy, Combination MeSH
- Rats MeSH
- Organophosphates MeSH
- Organophosphate Poisoning MeSH
- Oximes administration & dosage pharmacology MeSH
- Rats, Wistar MeSH
- Pyridinium Compounds administration & dosage pharmacology MeSH
- Cholinesterase Reactivators administration & dosage pharmacology MeSH
- Trimedoxime administration & dosage pharmacology MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Female MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't 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.
References provided by Crossref.org
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