Return of cholinesterase activity in the rat after inhibition by organophosphorus compounds. 2. A comparative study of true and pseudo cholinesterase

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Abstract
Evidence was presented to support the view that pseudo cholinesterase, like true cholinesterase, is phosphorylated by the organophosphorus compounds. The stability of the phosphorylated enzyme depends upon the enzyme inhibited and the organophosphate used. Some evidence was presented to suggest 2 types of true cholinesterase, differing in the stability of their phosphorylated active centers. The hydrolysis of phosphorylated pseudo cholinesterase is acid catalyzed; the hydrolysis of phosphorylated true cholinesterase is optimum at neutral pH. A working hypothesis was put forward suggesting that organophosphorus compounds combine with an amino group of pseudo cholinesterase, but that some other group is present in true cholinesterase.