Title : Mutant acetylcholinesterases as potential detoxification agents for organophosphate poisoning.

Pub. Date : 1997 Jul 15

PMID : 9271331






7 Functional Relationships(s)
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1 Here we report the effect of the corresponding mutation on the rate of inhibition, reactivation by 1-(2-hydroxyiminomethyl-1-pyridinium)-1(4-carboxyaminopyridinium)- dimethyl ether hydrochloride (HI-6), and aging of mouse AChE inhibited by C(+)P(-)- and C(-)P(-)-epimers of soman. asoxime chloride acetylcholinesterase Mus musculus
2 The E202 to Q mutation decreased the affinity of soman for AChE, slowed the reactivation of soman-inhibited AChE by HI-6, and decreased the aging of mutant AChE. asoxime chloride acetylcholinesterase Mus musculus
3 The E202 to Q mutation decreased the affinity of soman for AChE, slowed the reactivation of soman-inhibited AChE by HI-6, and decreased the aging of mutant AChE. asoxime chloride acetylcholinesterase Mus musculus
4 The E202 to Q mutation decreased the affinity of soman for AChE, slowed the reactivation of soman-inhibited AChE by HI-6, and decreased the aging of mutant AChE. asoxime chloride acetylcholinesterase Mus musculus
5 In vitro detoxification of soman and sarin by wild-type and E202Q AChE in the presence of 2 mM HI-6 showed that, E202Q AChE was 2-3 times more effective in detoxifying soman and sarin than wild-type AChE. asoxime chloride acetylcholinesterase Mus musculus
6 In vitro detoxification of soman and sarin by wild-type and E202Q AChE in the presence of 2 mM HI-6 showed that, E202Q AChE was 2-3 times more effective in detoxifying soman and sarin than wild-type AChE. asoxime chloride acetylcholinesterase Mus musculus
7 In vitro detoxification of soman and sarin by wild-type and E202Q AChE in the presence of 2 mM HI-6 showed that, E202Q AChE was 2-3 times more effective in detoxifying soman and sarin than wild-type AChE. asoxime chloride acetylcholinesterase Mus musculus