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Acetylcholinesterase and Butyrylcholinesterase Inhibited by Paraoxon

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    0333208 - ÚCHP 2011 RIV CH eng J - Journal Article
    Kuča, K. - Musilová, L. - Paleček, J. - Církva, Vladimír - Paar, M. - Musílek, K. - Hrabinová, M. - Pohanka, M. - Zdarová Karasová, J. - Jun, D.
    Acetylcholinesterase and Butyrylcholinesterase Inhibited by Paraoxon.
    Molecules. Roč. 14, č. 12 (2009), s. 4915-4921. E-ISSN 1420-3049
    Grant - others:MO0(CZ) FZV0000604
    Institutional research plan: CEZ:AV0Z40720504
    Keywords : acetylcholinesterase * reactivator * oxime
    Subject RIV: CC - Organic Chemistry
    Impact factor: 1.738, year: 2009

    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.
    Permanent Link: http://hdl.handle.net/11104/0178252

     
     
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