Abstract
The new bispyridinium oximes HI 6 and HLö 7 are promising antidotes against poisoning by highly toxic organophosphorus compounds, i.e. nerve agents. Until now, their ability to reactivate pesticide inhibited human acetylcholinesterase (AChE) has not been elucidated. For this purpose human erythrocyte AChE (EC 3.1.1.7) was inhibited (30 min) by chlorfenvinphos, dichlorvos, dicrotophos, heptenophos, mevinphos, monocrotophos, paraoxon, phosphamidon, trichlorfon, malaoxon, omethoate, oxydemeton-methyl or methamidophos by 85–98% of control. After removal of excess inhibitor, obidoxime, pralidoxime (2-PAM), HI 6 or HLö 7 (10, 30 or 100 μmol/l) were added and the AChE activity was measured spectrophotometrically at various times thereafter (5–60 min). The oximes significantly, but not completely, reactivated organophosphate inhibited AChE. The velocity and extent of reactivation were dependent on the oxime and its concentration. In all cases obidoxime was superior to the three other oximes, followed by HLö 7, 2-PAM and HI 6. In most cases obidoxime and HLö 7 were most effective at 10 or 30 μmol/l while 2-PAM and HI 6 needed 100 μmol/l. These data suggest that 2-PAM, HI 6 and HLö 7 are less patent than obidoxime in reactivating human AChE inhibited by organophosphate pesticides.
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Received: 25 August 1995/Accepted: 14 November 1995
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Worek, F., Kirchner, T., Bäcker, M. et al. Reactivation by various oximes of human erythrocyte acetylcholinesterase inhibited by different organophosphorus compounds. Arch Toxicol 70, 497–503 (1996). https://doi.org/10.1007/s002040050304
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DOI: https://doi.org/10.1007/s002040050304