Adsorption of human serum albumin to Amberlite XAD-7 resin.

In the present study the conditions leading to tight binding of human serum albumin to the Amberlite XAD-7 resin without the use of chemical coupling agents have been defined. Optimal binding (10.97 mm/kg dry XAD-7) was achieved at pH 5.0 and adsorption conformed to a Langmuir isotherm. Theoretical analysis of the data suggest adsorption of a monolayer of albumin which is supported by the absence of visual surface coating on scanning electron micrographs. Binding of human serum albumin was reduced when two chemical coupling agents, glutaraldehyde and carbodiimide were included in the human serum albumin solution, the elution of adsorbed HSA from the resins under severe flow conditions was reduced, and the amount eluted was minimal in all instances.