ANTIGEN-BINDING SITES DOMINATE THE SURFACE-PROPERTIES OF IGG ANTIBODIES

A new technique, liquid-liquid partition chromatography in an aqueous polyethylene glycol-dextran two-phase system, was used to detect diffe rences in surface properties of antibodies with different antigen-bind ing sites. Employing well-characterized monoclonal IgG antibodies and Fab and Fc fragments thereof as well as chimeric IgG antibodies we fou nd a remarkable relationship between structure of the antibody combini ng site and chromatographic behaviour. The surface properties of the I gG antibodies were dominated by those of its antigen-binding regions. In addition, our results indicated that the constant parts of the IgGs form similar scaffoldings, on to which CDRs of variable shapes and si zes are interspaced and constitute the major dominant differences in e xposed surface properties.