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A global kinetic analysis of a model of an autocatalytic zymogen-activation process in which an irreversible inhibitor competes with the zymogen for the active site of the proteinase is presented. Processes like the one here described are of great physiological interest because they are involved in the enzyme regulation of the gastrointestinal-tract enzymes, in blood coagulation, in fibrinolysis and in the complement system. The kinetic equations of both the transient phase and the steady state are derived for this mechanism. In addition, we have introduced a new parameter related to the kinetic behaviour of the system which allows us to predict whether the inhibition route or the activation route prevails in the steady state of the system. Finally, we extend the kinetic equations derived to different particular cases of the system studied.

Kinetic analysis of the control through inhibition of autocatalytic zymogen activation