Analysis of pH-induced changes of the glycolysis of human erythrocytes.

The full time courses of some important metabolites of the glycolysis of human erythrocytes are reported following pH-shifts from pH 7.4 to 8.1 and from 8.1 to 6.9. The regulatory enzymes which are affected by the pH-transitions have been identified by computer simulation using a mathematical model of the erythrocyte glycolysis. It is concluded that in the transition to pH 8.1 the hexokinase-phosphofructokinase system is activated and the pyruvate kinase is inhibited. At pH 6.9 the hexokinase-phosphofructokinase system and the bisphosphoglycerate mutase are inhibited whereas the non-glycolytic ATP-consuming processes seem to be activated.