Abstract
The kinetic properties of an open reconstituted enzyme system are investigated with the aim of demonstrating experimentally hysteretic transitions between alternate stationary states. The approach is based on a stirred flow-through reactor containing phosphofructokinase and pyruvate kinase entrapped in polyacrylamide gel. Through the reactor is pumped a solution containing fructose 6-phosphate, ATP, and phosphoenol pyruvate as well as adenylate kinase and glucose-6-phosphate isomerase. The latter two enzymes are in excess in respect to phosphofructokinase and pyruvate kinase. According to theoretical predictions the existence of multiple stationary states could be shown experimentally within precisely definable parameters. Switches between alternate stationary states have been caused by perturbations of flow rates and of reactant concentrations.
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