Interaction of phosphofructokinase with antibodies. Kinetic properties of phosphofructokinase in complexes with antibodies.
The allosteric properties of phosphofructokinase (EC 2.7.1.11) from rabbit muscle are influenced by enzyme concentration, most probably due to changes in the association state of the enzyme. In this study, the behaviour of dispersed pre-cipitates of phosphofructolinase as produced by treatment with antibodies has been investigated. The enzyme is not capable of rapid dissociation in the precipitated state as is confirmed by the lack of inactivation upon dilution and by the absence of shifts in substrate saturation curves as measured in the presence of different concentrations of the enzyme. The Hill coefficient of phosphofructokinase is decreased from 1.96 to 1.04 by antibody treatment. The V at neutral pH is increased 3-fold while the K0.5 for fructose 6-phosphate is reduced significantly. On the other hand, antibody-treated phosphofructokinase retains its sensitivity to allosteric activation by glucose 1,6-bisphosphate in the rpesence of high ATP concentrations.
D000494:Allosteric Regulation; D000818:Animals; D000906:Antibodies; D007700:Kinetics; D009132:Muscles / Q000201:enzymology; D010732:Phosphofructokinase-1 / Q000276:immunology / Q000378:metabolism*; D011233:Precipitin Tests; D011485:Protein Binding; D011817:Rabbits
D000906:Antibodies; D010732:Phosphofructokinase-1