Association of phosphofructokinase and aldolase with the membrane of the intact erythrocyte.
The binding of phosphofructokinase and aldolase to the membrane of the intact human erythrocyte was assessed by the rapid hemolysis/filtration method of Kliman and Steck (Kliman, H. J., and Steck, T. L. (1980) J. Biol. Chem. 255, 6314-6321). We found that about 50% of the phosphofructokinase was membrane-bound in fresh red cells prior to hemolysis. Binding was not significantly altered by deoxygenation. Approximately 40% of aldolase was membrane-associated in fresh red cells. In outdated, blood-banked red cells, aldolase was 73% membrane-bound while, following metabolic repletion, 40% of the enzyme was membrane-associated. These results support the hypothesis that certain glycolytic enzymes in the red cell are membrane-bound in a rapidly reversible and metabolically sensitive fashion.
D004910:Erythrocyte Membrane / Q000201:enzymology*; D005634:Fructose-Bisphosphate Aldolase / Q000097:blood*; D006461:Hemolysis; D006801:Humans; D007700:Kinetics; D009994:Osmolar Concentration; D010100:Oxygen / Q000378:metabolism; D010732:Phosphofructokinase-1 / Q000097:blood*; D012965:Sodium Chloride / Q000494:pharmacology
D012965:Sodium Chloride; D010732:Phosphofructokinase-1; D005634:Fructose-Bisphosphate Aldolase; D010100:Oxygen