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The use of empirical equations to describe dynamic dialysis “escape curves” in drug‐macromolecule binding measurements

The introduction of the dynamic dialysis technique to study the binding of small molecules to macromolecules (Meyer & Guttman, 1968; 1970a, b), has prompted a number of workers to utilize this approach in view of the apparent advantages inherent in this method (Dearden & Tomlinson, 1970; Goto, Ohki & others, 1971 ; Asghar & Roth, 1971; Brown & Crooks, 1973; Crooks & Brown, 1973; 1974a, b; Tukamoto, Ozeki & others, 1974). It became evident during studies utilizing this technique for the determination of the binding parameters of several steroidal anti-inflammatory agents and collagen (Kanfer, 1975), that methods available for obtaining the value of the slope of the curvilinear dynamic dialysis plot at various values of time in the presence of macromolecules, could lead to anomalies in the subsequent Scatchard plot. These values for the slope are necessary to obtain the instantaneous rate of escape at a value of Dt (total drug concentration) (Meyer & Guttman, 1968; 1970a). Meyer & Guttman (1968), in their original publication suggested that the slopes of the escape curve, in the presence of protein, at various values of time, could be estimated graphically. However, in view of the convenience and accuracy of fitting the data from plots of Dt versus time with the aid of a digital computer, the latter approach was employed by them. This involved the use of a six parameter tri-