RESUMO
The effect of the weak electric current (2 mA/cm2) on structural characteristics (hydrodynamic diameter and molecular weight) of the human serum albumin (HSA) was studied using photon correlation spectroscopy (PCS). The average diameter of initial HSA globule is approximately 7 nm (66.8 kDa). After electric current treatment during 2-5 min the diameter of HSA monomer increases to 7.5 nm. The duration of electric current treatment being increased to 20 min the size of HSA monomers decreases to 6.4 nm. The behaviour of HSA oligomers is close to that of monomers. Consequently, changes in the sizes of monomers and oligomers of HSA under the electric current treatment are caused by the change in the charge density stimulating change of tertiary structure of molecules and possible addition of ions from the buffer solution to them.