When bovine plasma albumin is in the presence of copper metal ions at pH values below the isoelectric point, a dimerization reaction takes place between the protein molecules. The kinetics of this reaction have been previously studied by using light scattering techniques. These techniques involve monitoring the amount of light scattered as the dimerization reaction proceeds. As the amount of dimer present increases, more light is scattered due to increased molecular size in the solution. Accurate calculations of the rate of this reaction depend upon knowing the ratio of dimer to monomer concentrations at any given time. Unfortunately, evidence has indicated that a small amount of trimer is also formed towards the end of this reaction. This complicates determination of the dimer concentration to the extent that definite conclusions cannot be drawn concerning reaction rates.
This study addresses the possibility of using ion exchange chromatography as a means of separating the BPA monomer, dimer, and trimer products so that their respective amounts can be more accurately determined. Hence, the data obtained will be a better reflection of the kinetics actually involved in this reaction
