Abstract
Interaction between bovine serum albumin and Co(II) cation was studied by equilibrium dialysis- differential refractometry, viscometry and dilatometry at different cobalt salt concentrations. Preferential absorption parameters and specific viscosity were determined from refractometric and viscometric measurements. This interaction produces structural changes in bovine serum albumin depending on the metal ion and protein concentrations. The results obtained by refractometric and viscometric techniques can be correlated with those deduced from dilatometric studies.
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