Hysteresis of Stationary States and Error Control in the Enzymatic Synthesis of DNA (poly‐dAT) in the Stirred Flow Reactor

Abstract

AbstractWith a stirred flow reactor we show for the first time that stationary states in open enzymatic systhesis of a simple DNA (poly‐dAT) by DNA polymerase I may be kinetically instable. Kinetic instabilities may lead to hysteresis of steady states. The concentrations of the DNA formed vary differentially in steady states that are established at ascending and descending volume rates of flow. The observed hysteresis loop is interpreted graphically. The synthetizing system has a simple chemical “memory” of its previous dynamic history. We show in a closed system that the inserting enzyme can not distinguish between a correct (adenine) and incorrect base (2‐aminopurine) at the beginning and end of the replication process. The specificities for the polymerase and hydrolysis activities are found to vary with time. A mechanism is proposed. We show that it is possible to regulate error incorporation of 2‐aminopurine monophosphate by the experimental choice of a stationary state in the stirred flow reactor.