SEPARATION OF BETA-LACTOGLOBULIN-A BY BIOSPECIFIC SUBUNIT EXCHANGE AFFINITY-CHROMATOGRAPHY

Studies were carried out to evaluate the separation of beta-lactoglobu lin A by biospecific subunit exchange affinity chromotography (BSEAC) and to measure the kinetics of the reaction. It was shown by a direct linear plot that there was more than one dissociation constant (Kd) wh ich indicated not only monomer/monomer interaction but also higher ord er aggregation during self-association. The Kd values were 104 mu Mol and 120 mu Mol for the dissociation of formed dimer and higher order a ggregates, respectively. The higher order aggregation during BSEAC was confirmed by hydrophobic interaction chromoatography (HIC). It has be en shown that BSEAC can be utilized to selectively separate beta-lacto globulin, however, further research is needed to define the conditions and specificity of separation from complex systems such as whey and m ilk.