Upward dead-end ultrafiltration of aqueous solutions of mixtures of bovine serum albumin (BSA) and egg white lysozyme was conducted using membranes which are almost completely retentive for BSA but permeable for lysozyme. The dependence of lysozyme rejection and the filtration flux rate on pH and the addition of salts has been investigated. The experimental data obtained in this study clearly demonstrate that the electrostatic interactions between dissimilar molecules may control the solute rejection and the filtration rate in upward ultrafiltration of binary protein mixtures. For instance, the BSA and lysozyme molecules have opposite electric charges at pH 7. Consequently, lysozyme rejection is large because both molecules within the filter cake pack more tightly due to heterocoagulation. On the other hand, the BSA and lysozyme molecules have the same electric charge at pH 4. Thus, lysozyme is rejected by the filter cake of the retained BSA molecules due to repulsive electrostatic interactions between the positively charged proteins. However, these charge effects weaken in the presence of salts. This study revealed that the solution environment can have profound effects upon solute and solvent transport in the ultrafiltration of binary protein mixtures.