EFFECT OF THE FORMATION OF INERT PROTEIN ON THE KINETICS OF THE AUTOCATALYTIC FORMATION OF TRYPSIN FROM TRYPSINOGEN

Abstract

A solution of crystalline trypsinogen in dilute buffer containing a trace of active trypsin when allowed to stand at pH 5.0–9.0 and 5°C. is gradually transformed partly into trypsin protein and partly into an inert protein which can no longer be changed into trypsin either by enterokinase or mold kinase. During the process of formation of trypsin and inert protein the ratio of the concentrations of the two products in any reaction mixture remains constant and is independent of the original concentration of trypsinogen protein. This ratio varies, however, with the pH of the solution, the proportion of trypsin formed being greater in the acid range of pH. The experimental curves for the rate of formation of trypsin, as well as for the rate of formation of inert protein are symmetrical S shaped curves closely resembling those of simple autocatalytic reactions. The kinetics of formation of trypsin and inert protein can be explained quantitatively on the theoretical assumptions that both reactions are of the simple unimolecular type, that in each case the reaction is catalyzed by trypsin, and that the rate of formation of each of the products is proportional to the concentration of trypsin as well as to the concentration of trypsinogen in solution.