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 differences in surface properties of antibodies with different antigen-binding sites. Employing well-characterized monoclonal IgG antibodies and Fab and Fc fragments thereof as well as chimeric IgG antibodies we found a remarkable relationship between structure of the antibody combining site and chromatographic behaviour. The surface properties of the IgG 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 sizes are interspaced and constitute the major dominant differences in exposed surface properties.
Wingren
C
C
Department of Biochemistry, University of Lund, Sweden.
Hansson
U B
UB
Magnusson
C G
CG
Ohlin
M
M
D000818:Animals; D002853:Chromatography, Liquid / Q000379:methods; D018604:Epitope Mapping; D000939:Epitopes / Q000737:chemistry*; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry* / Q000276:immunology; D007074:Immunoglobulin G / Q000737:chemistry* / Q000276:immunology; D051379:Mice; D013329:Structure-Activity Relationship
D000939:Epitopes; D007140:Immunoglobulin Fab Fragments; D007074:Immunoglobulin G