Abstract
Kinetics of inhibition of sheep red-cell cholinesterase by 6 substituted diethyl phenyl phosphate inhibitors were examined and shown to be 1st order and bimolecular. All the inhibitors examined contained as an impurity a small amt. of an active and unstable inhibitor of cholinesterase. This is in all probability tetraethyl pyrophosphate. A simple method of purification is given and the methods used to detect and determine tetraethyl pyrophosphate are given in detail. A relation between the stability of the inhibitors to aqueous hydrolysis at physiological pH and temp. and their power as inhibitors of cholinesterase was found. The more stable the inhibitor, the lower its inhibitory power. The mechanism of inhibition of cholinesterase by these compounds is discussed in relation to the above facts.