Figure 1. Presentation of data for the interaction of a univalent ligand with acceptor. (a) Simulated rectangular hyperbolic dependence of the binding function upon free ligand concentration (eqn (2)) for an acceptor with four sites (n = 4) governed by an intrinsic binding constant (K_AS) of 10⁵ mol L^–1. (b) Scatchard linear transformation (eqn (4a)) of the same dependence.

Figure 2. Allowance for ligand multivalence in the analysis of binding data. (a) Multivalent equivalent of the rectangular hyperbolic dependence of binding function upon free ligand concentration (eqn (6a)), simulated for a system with f = 2, n = 1, K_AS = 10⁵ mol L^–1 and [A]_tot = 20 mol L^–1. (b) General counterpart of the Scatchard plot (eqn (6b)) of the same dependence. (c) Conventional Scatchard plot of the same data.

Figure 3. Evaluation of binding constants by biosensor technology. Simulated time dependence of biosensor response resulting from injection (at 5 L min^–1) of 30 L of A (100 nmol L^–1) followed by buffer, B, (eqns (7a) and (8)) for a system with R_max = 3000 units, k_a = 10⁵ mol L^–1 s^–1 and k_d = 10^–2 s^–1. 1000 B/A core units = 0.1 degree. Inset: determination of the association and dissociation rate constants from the dependence of the pseudo-first-order rate constant (k_obs) upon the injected concentration of A (eqn (8)).