Antigen-binding sites dominate the surface properties of antibodies

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We have found a remarkable relationship between the specificity of antibodies and their chromatographic behavious upon liquid-liquid partition chromatography (LLPC). Well characterized human and murine monoclonal antibodies and Fab/Fv fragments thereof as well as mouse/human chimeric antibodies were employed.
While, lgG 1, 2 and 4 antibodies with identical specificities (affinity constants) have identical partition properties, lgG antibodies with different partition properties reacted with different partition epitopes or had different affinities against the same epitope. Hence, the surface properties of the antigen binding sites dominate over all other surfaces of the free antibody molecule.
LLPC may also be used to detect conformational changes occuring upon binding of antigen by antibody. Antigen-antibody complexes formed by different lgG antibodies against a large antigen like HSA all had similar surface properties. different from those of both antigen and antibody. In contrast, the surface properties of complexes formed by small antigens haptens are related to those of the lgG antibody.
In addition, antigen-antibody complexes were found to have similar surface properties irrespective of the molar ratio of antigen to antibody at which the complexes had been formed.


Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Immunology in the medical area
Original languageEnglish
Pages (from-to)276-276
Issue number4
StatePublished - 1996
Publication categoryResearch