1993 Volume 9 Issue 5 Pages 617-623
A solution of bovine serum albumin (BSA) was repeatedly injected into a column packed with EAH-Sepharose activated with glutaraldehyde (GA-activated Sepharose) at appropriate time intervals. The experimental elution profile of BSA from the column was analyzed by a model based on the assumption that BSA is bound to GA-activated Sepharose in two different modes. The mode having higher binding rate constant was attributed to an ionic interaction and the mode having lower rate constant was attributed to an aldehyde group on GA-activated Sepharose. These modes are distinguished in accordance with the effect of the ionic strength and pH of the carrier solution on the binding parameters of BSA. When the carrier solution had a lower ionic strength, the ionic interaction was a driving force for the binding of BSA. Once BSA was retained on the support by the interaction, BSA was subsequently bound to it more tightly by a bonding via an aldehyde group of GA-activated Sepharose. When a carrier solution containing 100mM NaCl was used, the ionic interaction was remarkably lowered. The pH 8 suitable for the formation of the binding via an aldehyde group gave a maximum amount in the dynamic binding process of BSA.