Structural Analysis of the Antibody Combining Site
The central problem of immunochemistry is to find the structural basis for antibody specificity. In view of the very wide range of different antigenic determinants and the overall similar basic structure of all antibodies the task seems formidable, and this problem has invited some paradoxical solutions in the past. However, it is now becoming increasingly apparent that the general architecture of antibody sites will not be different in principle from that of the active sites of enzymes. With the help of statistical analysis of amino acid sequences from myeloma proteins, affinity labeling of antibodies, and X-ray crystallographic analyses of crystals of antibody—hapten complexes, it seems that in the near future we will resolve the three-dimensional structure of an antibody site. It is already possible to speculate that in all antibodies the parts contributing to form the specific site are derived from similar sections of the variable region. I shall summarize here our studies which have had a role in the formation of this speculation and I shall discuss them in view of similar studies by others. In these studies we used both induced anti-DNP antibodies and mouse myeloma proteins with anti-DNP activity. The myeloma proteins are generally considered as representatives of homogeneous antibodies since in their reaction with DNP ligands they exhibit all the characteristics of binding sites of conventionally induced antibodies (Eisen et al., 1968).
KeywordsLight Chain Heavy Chain Hypervariable Region Myeloma Protein Affinity Label
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