Abstract
A coulometric-amperometric procedure was developed for the determination of the normality of α-chymotrypsin solutions. The procedure utilizes the specific inactivator, N,N-diphenylcarbamyl chloride as the titrant. Its reaction with active chymotrypsin releases one equivalent of chloride ion for every equivalent of enzyme inactivated. The chloride ion concentration, which, therefore, is equivalent to the concentration of active enzyme, is measured by a coulometric-amperometric procedure. As little as 0.1 μeq of enzyme at concentrations as low as 10 −4 M can be titrated with a precision of ±3%. It is suggested that this type of analytical procedure might be applicable for the titration of other enzyme systems.
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