An enzyme purified from squid nerve that hydrolyzes the cholinesterase inhibitor diisopropyl phosphorofluoridate (DFP) has now been coupled to agarose beads. A column of this agarose-DFPase hydrolyzes the nerve gas 1,2,2-trimethylpropyl methylphosphonofluoridate (Soman). Although the more inhibitory of the four diastereoisomers of Soman are hydrolyzed least rapidly, a column of sufficient length will accomplish 95 percent hydrolysis whether measured by fluoride release or loss of cholinesterase-inhibiting power. The results suggest a means for detoxifying unwanted chemical warfare agents.
Squid nerve contains an enzyme that hydrolyzes the nerve gas Tabun at about one-tenth the rate it hydrolyzes diisopropylphosphorofluoridate (DFP), and at about one-third to one-fourth the rate it hydrolyzes Sarin and Soman. Tabun is a more potent inhibitor of acetylcholinesterase than is DFP, is both lipid-and water-soluble, and penetrates readily into the squid giant axon in its inhibitory form. The failure of Tabun to block or markedly decrease the conducted action potential in the squid axon makes it likely that the blocking of conduction caused by DFP is probably not due to inhibition of acetylcholinesterase. Sub-strate specificity with regard to organophosphate metabolism by squid enzyme has possible implications for the disposal and detoxication of nerve gases in the ocean.
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