Nichol L W, Winzor D J
J Theor Biol. 1985 Dec 21;117(4):597-608. doi: 10.1016/s0022-5193(85)80241-1.
Explicit expressions are derived which describe the binding of a univalent ligand to equivalent and independent sites on each state of an acceptor undergoing indefinite self-association that is governed by an isodesmic equilibrium constant KI. From considerations of systems in which the same site-binding constant kA applies to all acceptor-ligand interactions, the general forms of binding curves and Scatchard plots are deduced for situations in which binding sites are either created or lost at each monomer-monomer interface. Greater generality is then introduced into the model by allowing ligand interactions with polymeric acceptor states to be governed by a site-binding constant kp that differs in magnitude from that for monomeric acceptor kA. Finally, experimental results with the glutamate dehydrogenase-GTP and lysozyme-saccharide systems are used to illustrate ways in which the present quantitative expressions may be applied to the characterization of inteactions between a ligand and an indefinitely self-associating acceptor.
