An extended model of the glycolysis in erythrocytes.
An extension of a previous model [2] is proposed of the glycolysis of erythrocytes which includes realistic rat laws for the hexokinase-phosphofructokinase system and for the 2,3-P2G phosphatase. Whereas most conclusions previously drawn are reinforced, the mechanism of ATP regulation is different in the present model. The ATP concentration is mainly regulated by the inhibitory action of ATP and the activating effect of AMP on the phosphofructokinase. The role of the 2,3-P2G bypass as a buffer of changes in the ATP demand is of lesser significance than previously thought. Besides the feedback action of the adenine nucleotides on the hexokinase-phosphofructokinase system in the quasisteady state the role of 2,3-P2G as an energy source is important since it can yield ATP for a certain period of time. The present version of the model describes qualitatively the experimental data on the modulation of Na+-K+-ATPase.
D000251:Adenosine Triphosphatases / Q000097:blood; D000255:Adenosine Triphosphate / Q000097:blood; D001676:Biofeedback, Psychology; D004912:Erythrocytes / Q000201:enzymology / Q000378:metabolism*; D006019:Glycolysis; D006593:Hexokinase / Q000097:blood; D006801:Humans; D010732:Phosphofructokinase-1 / Q000097:blood; D010735:Phosphoglycerate Kinase / Q000097:blood
D000255:Adenosine Triphosphate; D006593:Hexokinase; D010732:Phosphofructokinase-1; D010735:Phosphoglycerate Kinase; D000251:Adenosine Triphosphatases