Kinetic description of proteolysis. Part 3. Total kinetics of peptide bonds hydrolysis in peptide mixtures.

Abstract

A theoretical analysis of the general kinetics of peptide bond hydrolysis in peptide mixtures has been carried out. It is shown that the equation for the hydrolysis rate must include ensemble-averaged values which change as functions during hydrolysis. Thus the problem of describing the hydrolysis is reduced to finding these functions. As an example of theoretical prediction for the behavior of the averaged functions the procedure of calculating the averaged constant of chymotrypsin substrate specificity as a function of the degree of hydrolysis is presented. The analysis performed enables to find factors responsible for the decrease of hydrolysis rate, in particular, the role of the substrate specificity range and the S/E ratio. The design of specific experiments making it possible to measure the averaged values in the course of hydrolysis has been considered.