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It is shown that stable binding of a cholinesterase preparation to the surface of the hemoglobin-containing placenta-specific erythrocytes results in the change of its catalytic activity. Such binding occurs only at the optimum pH. The addition of chloroform to the erythrocyte suspension causes the loss of the catalytic activity of the enzyme preparation that has bound to the erythrocytes. The velocity of the enzyme inhibition by chloroform is practically identical to the one of the binding of the enzyme to the erythrocyte membrane. This inhibition effect is caused by the binding of the inhibitor to the enzyme molecule, and not by the interaction of chloroform with the enzyme-membrane complex. The conclusion on the similarity between the rates of specific enzyme binding to erythrocyte membrane and of enzyme inhibition by chloroform is postulated..
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