Enomoto A, Kamata N, Nakamura K
Department of Biological and Chemical Engineering, Faculty of Engineering, Gunma University, Japan.
Biochem Biophys Res Commun. 1994 Jun 15;201(2):1008-13. doi: 10.1006/bbrc.1994.1802.
A suitable antibody for immunoaffinity chromatography is considered to efficiently bind the antigen in the adsorption step and to dissociate the bound antigen with mild changes in the environmental conditions. To develop an effective method for preparing such antibodies, murine antisera elicited by the primary and secondary responses against bovine beta-lactoglobulin, a model protein antigen, were examined and compared for their ability to bind the antigen under differing pH and ionic strength conditions. Antibodies from the primary response were usually found to be highly sensitive to changes in pH and ionic strength, suggesting that these antibodies may be useful as ligands for immunoaffinity chromatography.
