Comparison of Sepharose CL-2B and CL-4B Matrices in Purification of the Hepatitis B Surface Antigen by Affinity Chromatography

Sepharose CL-4B and Sepharose CL-2B with immobilized CB.Hep-1 monoclonal antibody were compared for studying the matrix efficiency in the immunopurification of the recombinant hepatitis B surface antigen (rHBsAg). The elution capacities of both matrices were similar over eight chromatographic cycles, significant differences were only observed in the first purification cycles. A high percentage of the adsorbed rHBsAg was not eluted from both matrices. The rHBsAg purity was not affected by matrix characteristics (pore size and percentage of agarose) and differences between Sepharose CL-4B and Sepharose CL-2B do not provoke differences in the antibody released from the matrices under defined experimental conditions.