Abstract
In this paper, an analysis of the influence of the salt types, NaCl, NaCH 3COO, Na 2SO 4 and Na 3C 6H 5O 7, on the isocratic retention behaviour of bovine serum albumin (BSA) on two anion-exchangers media (Source 30Q and TSK Gel Super Q 5 PW) has been presented. The retention data demonstrated that the mechanism of protein retention in ion-exchange chromatography (IEC) involves interactions between the protein solute, the mobile phase constituents and the stationary phase. The effect of protein activity coefficient in the mobile phase on the protein retention volumes is verified.
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