[Simulation of the kinetics of oligomeric enzymes as illustrated by phosphofructokinase. I. General analysis of experimental data and the choice of an adequate model].
On the example of complex allosteric kinetics of phosphofructokinase from human erythrocytes we analysed the applicability of the Monod-Wyman-Changeux and association--dissociation models to the unified description of the kinetics of the oligomeric enzymes. It was shown that these models were not sufficient to construct an adequate phosphofructokinase model. We propose to use the unidimensional Izing model for this purpose. It was analysed in the monosubstrate case for the high enzyme concentration range. The ways to generalize the Izing model as the basis of the universal model for the oligomeric enzyme's kinetics were analysed.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000494:Allosteric Regulation; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D008954:Models, Biological; D010732:Phosphofructokinase-1 / Q000037:antagonists & inhibitors / Q000097:blood / Q000378:metabolism*; D013379:Substrate Specificity
D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1
Modelirovanie kinetiki deĭstviia oligomernykh fermentov na primere fosfofruktokinazy. I. Obshchiĭ analiz éksperimental'nykh dannykh i vybor adekvatnoĭ modeli.