Kinetic behavior of associating enzyme systems ofthe type M in equilibrium M2 in equilibrium M3 in equilibrium ... and of the type 2M in equilibrium D in equilibrium D2 in equilibrium D3 in equilibrium ...
A theoretical analysis has been made of dependencies of specific enzymatic activity (a) on the concentration of the enzyme for associating enzyme systems, in which the association of protein molecules leads to the formation of linear associates of an unlimited length (M in equilibrium M2 in equilibrium M3 in equilibrium ...) and is accompanied by steric shielding of active centers, and also for systems of the type 2 M in equilibrium D in equilibrium D2 in equilibrium D3 in equilibrium ... (M is an inactive monomer and D is an active dimer), in which the specific enzymatic activity of the dimer does not depend on the degree of association. For both models an analysis has been made of the S-shape of the curves of the dependence of a on the concentration of the substrate. Experimental data for glutamate dehydrogenase from ox liver and phosphofructokinase from rabbit skeletal muscles have been used as illustrations.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004798:Enzymes / Q000378:metabolism*; D005969:Glutamate Dehydrogenase / Q000378:metabolism; D005971:Glutamates; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D046911:Macromolecular Substances; D008433:Mathematics; D008722:Methods; D009132:Muscles / Q000201:enzymology; D010732:Phosphofructokinase-1 / Q000378:metabolism; D011485:Protein Binding; D011817:Rabbits
D004798:Enzymes; D005971:Glutamates; D046911:Macromolecular Substances; D005969:Glutamate Dehydrogenase; D010732:Phosphofructokinase-1