Add time:09/05/2019         Source:sciencedirect.com

1.1. In addition to its primary role as regulator of hemoglobin oxygenation, 2,3-diphosphoglyceric acid has been cited as an inhibitor of several enzymes in the erythrocyte. In this paper four enzymes of glycolysis [hexokinase (ATP:d:hexose 6-phosphotransferase, EC 2.7.1.1), phosphofructokinase (ATP:d-fructose 6-phosphate I-phosphotransferase, EC 2.7.1.11), phosphoglycerate kinase (ATP:3-phospho-d-glycerate I-phosphotransferase, EC 2.7.2.3), and pyruvate kinase (ATP: pyruvate phosphotransferase, EC 2.7.1.40) were partially purified from the human red blood cell and the effect of 2,3-diphosphoglycerate upon their activities was measured.2.2. It was demonstrated that in addition to hexokinase, about which there had been conflicting previous reports, the other three kinases are inhibited at normal intracellular levels of 2,3-diphosphoglycerate, but that a marked variation in sensitivity exists.3.3. Kinetic studies of this inhibition reveal that generally 2,3-diphosphoglycerate is competitive with ATP, ADP, or the ATP-2 Mg2+ complex. A tabular summary of the Ki and Km values for these enzymes is given.4.4. It is concluded from these experiments together with studies on glucose utilization by cells containing varying amounts of 2,3-diphosphoglycerate that inhibition of hexokinase is probably the most significant step in regulation of glycolysis by 2,3-diphosphoglycerate.5.5. The competitive effect between, 2,3-diphosphoglycerate and ATP on these four kinases and its possible significance in mammalian erythrocytes is discussed briefly.

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