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Reactivation of Human Brain Homogenate Cholinesterases Inhibited by Tabun using Newly Developed Oximes K117 and K127
Author(s) -
Kuca Kamil,
Cabal Jiri,
Jung Yung Sik,
Musilek Kamil,
Soukup Ondrej,
Jun Daniel,
Pohanka Miroslav,
Musilova Lucie,
Karasová Jana,
Novotný Ladislav,
Hrabinova Martina
Publication year - 2009
Publication title -
basic and clinical pharmacology and toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.805
H-Index - 90
eISSN - 1742-7843
pISSN - 1742-7835
DOI - 10.1111/j.1742-7843.2009.00421.x
Subject(s) - tabun , oxime , pralidoxime , acetylcholinesterase , chemistry , pharmacology , in vivo , potency , in vitro , human brain , aché , enzyme , biochemistry , biology , neuroscience , microbiology and biotechnology
Newly developed acetylcholinesterase reactivators K117 [1,5‐bis(4‐hydroxyiminomethylpyridinium)‐3‐oxapentane dichloride] and K127 [(1‐(4‐hydroxyiminomethylpyridinium)‐5‐(4‐carbamoylpyridinium)‐3‐oxapentane dibromide)] were tested for their potency to reactivate tabun‐inhibited human brain cholinesterases. Pralidoxime and trimedoxime were chosen as standard reference reactivators. Human tissue was used, as that was closer on the real treatment of human beings. As a result, oxime K127 was found as the best tested reactivator according to the constant k r , characterizing the overall reactivation process. On the contrary, the maximal reactivation ability expressed as percentage of reactivation was the best for trimedoxime. This differences were caused as a result of using the enzyme from different species. Due to this, experiments on human tissue should be conducted after in vitro and in vivo tests on animals to eliminate such important failures of promising oximes.