Mechanism of aldolase binding to erythrocyte membrane: Part II. Kinetic aspects.
The nature of binding of FDP aldolase to bovine erythrocyte membrane was examined. The Km value of bound and soluble enzyme differed by an order. The absence of time-lag in the velocity-time curves at various concentrations of the substrate and the similar extent of inactivation of bound and soluble enzyme on heat treatment suggested that the enzyme was bound at a point other than the catalytic site. The release of the enzyme by various glycolytic intermediates suggested their involvement in binding to the catalytic site through phosphate linkage. The non-phosphorylated compounds like lactate, reduced glutathione, 2-mercaptoethanol and EDTA were ineffective in eluting the enzyme. On the basis of separate binding sites on the enzyme for membrane and ligands, the mechanism of association dissociation of aldolase has been suggested.
D000818:Animals; D002384:Catalysis; D002417:Cattle; D003593:Cytoplasm / Q000201:enzymology; D004355:Drug Stability; D004910:Erythrocyte Membrane / Q000201:enzymology*; D005634:Fructose-Bisphosphate Aldolase / Q000037:antagonists & inhibitors / Q000097:blood*; D006019:Glycolysis; D006358:Hot Temperature; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D011485:Protein Binding; D011817:Rabbits
D005634:Fructose-Bisphosphate Aldolase