The specificity of cobra-venom cholinesterase

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Abstract
The hydrolysis of choline and non-choline esters by cobra venom was studied. All hydrolysis was attributed to cholinesterase. It was suggested that the enzyme was inactivated at interfaces giving an erroneous idea of the specificity pattern when sparingly soluble esters were used. The enzyme was, however, protected by the addition of gum acacia or inert proteins. The protected enzyme give a specificity pattern similar to those found for other acetocholinesterases. Acetates were hydrolyzed faster than the corresponding propionates; butyrates were not hydrolyzed. The rate of hydrolysis of aliphatic esters increased as the acetylcholine configuration was approached, giving a max.