The simple Langmuir isotherm is frequently employed to describe the equilibrium behavior of protein adsorption on a wide variety of adsorbents. The two adjustable parameters of the Langmuir isotherm - the saturation capacity, or $q_m$, and the dissociation constant, $K_d$ - are usually estimated by fitting the isotherm equation to the equilibrium data acquired from batch equilibration experiments. In this study, we have evaluated the possibility of estimating $q_m$ and $K_d$ for the adsorption of bovine serum albumin to a cation exchanger using batch kinetic data. A rate model predicated on the kinetic form of the Langmuir isotherm, with three adjustable parameters ($q_m,;K_d$, and a rate constant), was fitted to a single kinetic profile. The value of $q_m$ determined as the result of this approach was quantitatively consistent with the $q_m$ value derived from the traditional batch equilibrium data. However, the $K_d$ value could not be retrieved from the kinetic profile, as the model fit proved insensitive to this parameter. Sensitivity analysis provided significant insight into the identifiability of the three model parameters.