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Acetylcholinesterase and Butyrylcholinesterase Inhibited by Paraoxon
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SYSNO ASEP 0333208 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Acetylcholinesterase and Butyrylcholinesterase Inhibited by Paraoxon Author(s) Kuča, K. (CZ)
Musilová, L. (CZ)
Paleček, J. (DE)
Církva, Vladimír (UCHP-M) RID, ORCID, SAI
Paar, M. (CZ)
Musílek, K. (CZ)
Hrabinová, M. (CZ)
Pohanka, M. (CZ)
Zdarová Karasová, J. (CZ)
Jun, D. (CZ)Source Title Molecules. - : MDPI
Roč. 14, č. 12 (2009), s. 4915-4921Number of pages 7 s. Language eng - English Country CH - Switzerland Keywords acetylcholinesterase ; reactivator ; oxime Subject RIV CC - Organic Chemistry CEZ AV0Z40720504 - UCHP-M (2005-2011) UT WOS 000273043200009 DOI 10.3390/molecules14124915 Annotation Four novel bisquaternary aldoxime cholinesterase reactivators differing in their chemical structure were prepared. Afterwards, their biological activity was evaluated for their ability to reactivate acetylcholinesterase (AChE; EC 3.1.1.7) and butyrylcholinesterase (BuChE; EC 3.1.1.8) inhibited by paraoxon. Their reactivation activity was compared with standard reactivators—pralidoxime, obidoxime and HI-6—which are clinically used at present. As it resulted, none of the prepared compounds surpassed obidoxime. In case of BuChE reactivation, two compounds (K053 and K068) achieved similar results as obidoxime. Workplace Institute of Chemical Process Fundamentals Contact Eva Jirsová, jirsova@icpf.cas.cz, Tel.: 220 390 227 Year of Publishing 2011
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