Investigation of serum-albumin aggregation

It has been revealed by dynamic light scattering that human bloodplasma serum albumin (HAS) aggregates in the presence of heavymetal salts (CsCl) and the size of the HSA aggregates depends linearly on the salt concentration. A parabolic dependence of the hydrodynamic radius of the HSA particles on the pH level of an HSA buffer solution with a maximum at the isoelectric point of HSA (pI 5.0) has been obtained. It has been established that aggregates of HSA molecules represent ellipsoids of revolution which are transformed into practically spherical complexes on addition of CsCl to a solution.