Eschrich K, Schellenberger W, Hofmann E
Acta Biol Med Ger. 1982;41(5):415-24.
The kinetic behavior of a reconstituted eyzyme system containing purified phosphofructokinase, pyruvate kinase, adenylate kinase, and glucose 6-phosphate isomerase was investigated. Experimentally the approach is based on a stirred flow-through reactor containing gel entrapped enzymes. The experiments were performed on the basis of a mathematical model developed from the kinetic properties of the individual enzymes involved. The system is able to exhibit alternative stable stationary states for one set of experimental conditions (bistability) originating mainly from the allosteric character of the phosphofructokinase. From a functional point of view, these states are either ATP-generating or ATP-consuming. Theoretically, the appearance of alternate steady states gives rise to hysteretic behavior of the system. In fact, transitions between alternate ATP generating stationary states as well as between ATP-generating and ATP-consuming steady states were observed experimentally.
研究了一种重组酶系统的动力学行为，该系统包含纯化的磷酸果糖激酶、丙酮酸激酶、腺苷酸激酶和葡萄糖6-磷酸异构酶。实验方法基于一个装有凝胶包埋酶的搅拌式流通反应器。实验是基于从所涉及的各个酶的动力学特性建立的数学模型进行的。该系统在一组主要源于磷酸果糖激酶变构特性的实验条件下能够表现出交替稳定的稳态（双稳态）。从功能角度来看，这些状态要么是产生ATP的，要么是消耗ATP的。理论上，交替稳态的出现会导致系统的滞后行为。事实上，实验中观察到了交替的产生ATP稳态之间以及产生ATP和消耗ATP稳态之间的转变。
