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. Author manuscript; available in PMC: 2017 May 1.
Published in final edited form as: Int J Toxicol. 2016 Apr 21;35(3):344–357. doi: 10.1177/1091581816638086

Figure 1. In vitro, 2-PAM Cl does not reactivate gpAChE-R when inhibited by a carbamate.

Figure 1

Using the Ellman’s based assay, the reactivation of gpAChE-R by 2-PAM Cl, against the experimentally determined IC95 of aldicarb (509 μM), methomyl (174 μM), or sarin (GB) (0.475 μM) was evaluated. Unchallenged gpAChE-R was used to determine maximum activity. To more closely mimic the in vivo study, at one minute post-challenge 2-PAM Cl was added at a final concentration of (A) 10 μM or (B) 100 μM. The indicator and substrate were added at 0, 0.5, 1, 2, 4, or 24 h and read immediately to determine activity. Activity is represented as a percentage of the unchallenged control. Data shown are mean ± SEM, representing n ≥ 5. For both carbamates but not GB, both treatment levels of 2-PAM Cl significantly contributed to additional enzyme inhibition. For GB, both treatment levels of 2-PAM Cl significantly ameliorated enzyme inhibition. gpAChE-R remained relatively stable for the duration of the 24 hour incubation as ≤ 15% decrease in activity was observed as compared to T=0 hours (data not shown).