Mean activity coefficients of different potassium salts KX (X = F-, Cl-, Br-, I-, NO3-, SCN-) have been measured in concentrated isoionic bovine serum albumin (BSA) solutions, by use of the EMF method with ion-exchange membrane electrodes. These solutions may be regarded as simple model systems for the cytoplasm of living cells as far as the influence of the macromolecular component on the activity coefficients of the salts is concerned. Two series of measurements have been carried out: (a) varying the amount of salt from 0.01 to 0.5 molal and maintaining the BSA concentration constant at 20 wt% and (b) varying the protein concentration up to 25 wt% and keeping the salt concentration constant at 0.1 molal. For all salts studied, the mean activity coefficients in the protein-salt solutions increase as the salt concentration rises, when the protein concentration is maintained constant. In the series of measurements (b) the activity coefficients of all salts change linearly with the protein concentration. Marked qualitative differences, however, were observed depending on the anion species, which could be interpreted in terms of specific ion binding of X- to the protein molecule. By taking into account BSA-bound 'non-solvent' water, the results were analyzed in terms of numbers of anions bound per BSA molecule. Comparison with the results of Scatchard, obtained at low protein concentrations, showed only a very small electrostatic effect of the BSA-(X-)v polyions on the activity coefficient of the salts at higher protein and salt concentrations.