Mathematical analysis of multienzyme systems. I. Modelling of the glycolysis of human erythrocytes.
A mathematical model for the glycolysis of human erythrocytes is presented which takes into account ATP-synthesis and -consumption. A set of three differential equations describes the steady states and the time-dependent changes of the metabolite concentrations under blood storage conditions. For a given parameter combination there are in general three stationary points of the system, one of which is unstable. At a low ATP-need the ATP-level is relatively constant for variations in the rate constant of the ATP-consuming processes. Above a critical level of the energy consumption the system breaks down. An important role of the 2.3P2G-bypass of the erythrocytes is its action as an "energy buffer", wasting ATP in case of ATP-overproduction and producing ATP in case of underproduction. A parameter combination consistent with the data on the isolated enzymes was found which gives a good agreement of theoretical predictions with the measured metabolite concentrations. Under blood preservation conditions the difference of the rates of ATP-production and -consumption is the most important factor for a high ATP-level over long periods.
D000251:Adenosine Triphosphatases / Q000097:blood; D001731:Bisphosphoglycerate Mutase / Q000097:blood; D004163:Diphosphoglyceric Acids; D004912:Erythrocytes / Q000201:enzymology*; D006019:Glycolysis; D006593:Hexokinase / Q000097:blood; D006801:Humans; D007700:Kinetics; D008433:Mathematics; D008954:Models, Biological; D010732:Phosphofructokinase-1 / Q000097:blood; D010744:Phosphoric Monoester Hydrolases / Q000097:blood; D011770:Pyruvate Kinase / Q000097:blood
D004163:Diphosphoglyceric Acids; D006593:Hexokinase; D010732:Phosphofructokinase-1; D011770:Pyruvate Kinase; D010744:Phosphoric Monoester Hydrolases; D000251:Adenosine Triphosphatases; D001731:Bisphosphoglycerate Mutase