Small angle neutron scattering study reveals that at pD ≈ 7.0, above the isoelectric point of the globular protein Bovine Serum Albumin (BSA), in the presence of different divalent ions (Mg²⁺, Ca²⁺, Sr²⁺ and Ba²⁺), the short-range attractive interaction remains nearly constant and the intermediate-range repulsive interaction decreases with increasing salt concentration up to a certain concentration value but after that remains unchanged. However, for the monovalent ion (Na⁺), repulsive interaction decreases gradually up to 1 M salt concentration. Dynamic light scattering study shows that for all ions, diffusion coefficient of BSA decreases with increasing salt concentration and then nearly saturates.