[Hysteresis and multiplicity of dynamic states in open 2-substrate enzyme reactions with substrate inhibition].

A mathematical model of an open two-substrate enzymic with substrate inhibition has been analyzed. The hysteretic form of the reaction input characteristics resulting in the appearance of three alternative stationary states, O1, O2 and O3, has been obtained. The region of existence of a stable limit cycle has been determined within the framework of linear approximation. Analysis of the model to a non-linear approximation shows that close to the boundary of the stability region the unstable or stable limit cycle can surround O1 or O3 as well as the only stationary state O.