Influence of 2,3-diphosphoglycerate on phosphofructokinase of human erythrocytes?

Abstract

Phosphofructokinase catalyzes the conversion of fructose-6-phosphate to fructose-1,6-diphosphate. Control of glycolysis is usually explained in terms of the properties of three enzymes: hexokinase, phosphofructokinase and pyruvate kinase. Recently Beutler reported that phosphofructokinase (PFK) of human erythrocytes is inhibited by 2,3-DPG. It is known that the concentration of 2,3-DPG in erythrocytes is very high. In view of control of glycolysis the finding by Beutler is very important. However, our results are in disagreement with those of Beutler.