[Kinetic manifestations of slow isomerization of allosteric enzyme for the model of Monod, Wyman and Changeux].

A shape of the curves of a product accumulation in time (t) is analysed for the variant of Monod, Wyman and Changeux model which is characterized by comparable rates of equilibration between R and T enzyme forms on the one hand and the enzymatic process on the other hand. It is assumed that the complex of R and T forms with substrate are in rapid equilibrium with the free components. The character of the dependences of effective constant of R denoting T isomerization and the value of tau on substrate concentration are analysed (tau is the intercept of t-axis for linear asymptota of the curve of product concentration versus time at t leads to infinity). It is also shown that the low rate of R denoting T isomerization may be manifested by the shape of the plot of initial reaction rate versus substrate concentration unusual for the model of Monod et al. (the plots with intermediate plateau and ones with Hill's coefficient of cooperativity less than unity).