The paper gives a summary of successful methods for measuring protein mass transfer kinetics in ion exchange matrices along with models needed to interpret experimental results. Both macroscopic methods (isocratic elution, gradient elution, batch adsorption, frontal analysis) and microscopic methods are considered. In all cases the main focus is the determination of the effective intrapartide diffusivity in order to permit a comparison of different stationary phases and provide a basis for predicting chromatographic process performance. Experimental results for representative systems are evaluated alongside the experimental and modeling aspects. Practical criteria for the selection of experimental conditions and the application of different models are discussed along with the advantages and disadvantages of the various approaches.