Abstract
Abstract: In the presence of oximes phenylthioacetate is deacetylated and acetylated oximes formed. By measuring the velocity of this transacetylation reaction for a number of oximes in vitro, the slopes are found to differ in a way which resembles the variance in the potency of the oximes in vivo as reactivators for cholinesterases inhibited by alkyl organophosphorous compounds. The observations thus support the hypothesis that oximes as acetyl acceptors might have an effect by inhibition of the synthesis of acetylcholine due to deacetylation of acetyl‐coenzyme‐A.
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