title: Association of phosphofructokinase and aldolase with the membrane of the intact erythrocyte.
abstract: 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 In outdated, blood-banked red cells, aldolase was 73% membrane-bound while, following metabolic repletion, 40% of the enzyme was membrane-associated.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.
mesh_terms: 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
chemical_list: D012965:Sodium Chloride; D010732:Phosphofructokinase-1; D005634:Fructose-Bisphosphate Aldolase; D010100:Oxygen