Abstract
Summary
The acetyl ester of thiamine chloride was found to be a poorer inhibitor of choline esterase than free thiamine, while the pyrophosphoric ester had even less inhibitory action. The affinity for the enzyme of the former was calculated to be 5.3, and of the latter 1.7, times that of acetylcholine. The acetyl ester was hydrolyzed slowly by horse serum, the magnitude of the enzymatic splitting being approximately equal to that due to the hydroxylion scission at the same pH (7.4).
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