The theoretical analysis of kinetic behaviour of “hysteretic” allosteric enzymes. II. The dissociating and associating enzymic systems in which the rate of installation of equilibrium between the oligomeric forms is small in comparison with that of enzymatic reaction

The present paper is concerned with the specificities of kinetic behaviour of dissociating enzyme systems where the equilibrium between oligomeric forms installs rather slowly in comparison with the rate of enzymatic reaction. In the slowly dissociating enzyme systems of the type Np ? P (P is enzyme oligomer and p is a subunit; N ? 2) in which the forms P and p exhibit different allosteric interactions between active and allosteric sites the initial rate of enzymatic reaction (v) versus the substrate concentration (S) or the effector concentration (F) were shown to be of rather complex pattern. In similar systems the v versus [S]₀ plots may show an intermediate plateau, maximum and minimum simultaneously, an intermediate plateau and its preceding S-shape, etc., as well as v versus [F]₀ may show an intermediate plateau.