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.
D000244:Adenosine Diphosphate / Q000097:blood; D000255:Adenosine Triphosphate / Q000097:blood; D001786:Blood Glucose / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism*; D005635:Fructosediphosphates / Q000097:blood; D005958:Glucosephosphates / Q000097:blood; D006019:Glycolysis; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics
D001786:Blood Glucose; D005635:Fructosediphosphates; D005958:Glucosephosphates; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate