Open AccessKinetic analysis of zymogen autoactivation in the presence of a reversible inhibitor
Author(s) -
Wang WeiNing,
Pan XianMing,
Wang ZhiXin
Publication year - 2004
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.2004.04416.x
Subject(s) - zymogen , benzamidine , proteolysis , trypsinogen , chemistry , autocatalysis , proteases , protease , enzyme , trypsin , biochemistry , stereochemistry , catalysis
Limited proteolysis is a highly specific irreversible process, which can serve to initiate physiological function by converting a precursor protein into a biologically active form. When the activating enzyme and the activated enzyme coincide, the process is an autocatalytic zymogen activation (i.e. reactions in which the zymogens serves as a substrate for the corresponding active enzyme). The activity of proteases is frequently regulated by the binding of specific protease inhibitors. Thus, to understand the biological regulation of proteolysis, one must understand the role of protease inhibitors. In the present study, a detailed kinetic analysis of autocatalytic reaction modulated by a reversible inhibitor is represented. On the basis of the kinetic equation, a novel procedure is developed to evaluate the kinetic parameters of the reaction. As an example of the application of this method, effects of acetamidine, p ‐amidinobenzamidine and benzamidine on the autoactivation of trypsinogen by trypsin were studied.