Reactivation of human acetylcholinesterase and butyrylcholinesterase inhibited by leptophos-oxon with different oxime reactivators in vitro.

Autor: Jun D; Faculty of Military Health Sciences, University of Defence, Hradec Kralove, Czech Republic., Musilova L, Pohanka M, Jung YS, Bostik P, Kuca K
Jazyk: angličtina
Zdroj: International journal of molecular sciences [Int J Mol Sci] 2010 Aug 03; Vol. 11 (8), pp. 2856-63. Date of Electronic Publication: 2010 Aug 03.
DOI: 10.3390/ijms11082856
Abstrakt: We have evaluated in vitro the potency of 23 oximes to reactivate human erythrocyte acetylcholinesterase (AChE) and plasma butyrylcholinesterase (BChE) inhibited by racemic leptophos-oxon (O-[4-bromo-2,5-dichlorophenyl]-O-methyl phenyl-phosphonate), a toxic metabolite of the pesticide leptophos. Compounds were assayed in concentrations of 10 and 100 μM. In case of leptophos-oxon inhibited AChE, the best reactivation potency was achieved with methoxime, trimedoxime, obidoxime and oxime K027. The most potent reactivators of inhibited BChE were K033, obidoxime, K117, bis-3-PA, K075, K074 and K127. The reactivation efficacy of tested oximes was lower in case of leptophos-oxon inhibited BChE.
Databáze: MEDLINE