Schellenberger W, Eschrich K, Hofmann E
Eur J Biochem. 1981 Aug;118(2):309-14. doi: 10.1111/j.1432-1033.1981.tb06403.x.
The self-stabilization of the energy charge and of ATP was investigated in an open reconstituted enzyme system containing phosphofructokinase, pyruvate kinase, adenylate kinase, and glucose-6-phosphate isomerase. The experiments were performed in a stirred flow-through reactor containing gel-entrapped enzymes. The dynamics of the system were analyzed theoretically by a model based on the kinetic properties of the individual enzymes. The energy charge was identified as one of the essential variables of the system. According to the theoretical prediction, homoeostasis of the energy charge was observed experimentally when either the maximal activity of phosphofructokinase, the energy charge of the influx solution of the flow rate through the reaction chamber was varied. It is shown that the efficiency of stabilization of the energy charge is related to the occurrence of alternative stationary states.
在一个包含磷酸果糖激酶、丙酮酸激酶、腺苷酸激酶和葡萄糖-6-磷酸异构酶的开放重组酶系统中，研究了能量电荷和ATP的自我稳定。实验在一个含有凝胶包埋酶的搅拌式流通反应器中进行。通过基于各酶动力学特性的模型对系统动力学进行了理论分析。能量电荷被确定为系统的基本变量之一。根据理论预测，当磷酸果糖激酶的最大活性、反应室流入溶液的能量电荷或流速发生变化时，实验中观察到了能量电荷的稳态。结果表明，能量电荷稳定的效率与交替稳态的出现有关。
