Abstract
The binding equilibria of antibody and hapten are usually characterized by a single step mechanism. This simple mechanism enabled the detailed analysis of molecular recognition in kinetic terms. Still this mechanism does not always prevail and a number of homogeneous immunoglobulins of known specificity, which exhibit conformational transitions induced by hapten binding, have by now been observed. One of these immunoglobulins (MOPC 460) is found to exist in two conformational states, both when free or hapten bound. The transition between the different states is induced by the hapten binding.
Following the circular polarization of the intrinsic fluorescence of the antibodies, the induction of conformational changes upon antigen binding has been shown to be transmitted to the Fc domains. The examination of these spectroscopic changes has now been extended and correlated with the induction of complement binding. For antibodies of the IgG class a correlation was found only when divalent or polyvalent antigens were bound, whereas for IgM class antibodies of the same specificity, binding of the monovalent antigenic determinant was sufficient for both activation of complement and induction of the changes in circular polarization of luminescence (CPL).
These observations support the notion that the interaction between the antigen binding site and the effector sites of antibodies have an allosteric nature. The significance of the requirement of antigen divalency for IgG may be an inherent part of this nature so as to accommodate an appropriate angular relation between the different domains of the immunoglobulin molecule.
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Pecht, I. (1976). Recognition and Allostery in the Mechanism of Antibody Action. In: Melchers, F., Rajewsky, K. (eds) The Immune System. Colloquium der Gesellschaft für Biologische Chemie, vol 27. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-81083-1_4
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DOI: https://doi.org/10.1007/978-3-642-81083-1_4
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