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81:3155. A. E. D. Gottlieb, U. J. Waxdal. 1969. The covalent structure of an entire yG1 immunoglobulin molecule. Biochemistry 63: 78-85. Hilschmann, N. C. Craig. 1965. Amino acid sequence studies with Bence-Jones proteins. Biochemistry 53: 1403-1409. M. D. Capra. 1971. Localization of two additional hypervariable regions in immunoglobulin heavy chains. Proc. Natl. Acad. Sci. 68: 20192021. M. P. L. P. Phizackerley, and F. Saul. 1973. 8-A resolution. Proc. Natl. Acad. Sci. 70: 3305-3310. Porter, et al.

This reaction is an intramolecular conversion and does not depend on diffusion. It is restrained only by conformation (Fig. 2). Once this molecular complex is assembled, the rate of dissociation of the individual antibodyepitope interactions is ·similar to the normal bimolecular complex. However, since the antigen will still be held by the other interaction, HIGH AVIDITY . 2 Bivalent binding of antibodies to polymeric antigens increases the avidity. 3 Polyclonal antibodies binding to multivalent antigens.

Antibodies that bind to multiple sites on an antigen can form large, stable, multimeric complexes When an antigen with more than one epitope is mixed with polyclonal antibodies, the complexes that form can be stabilized by intermolecular bridges (Fig. 3). During complex formation, one antibody binds more than one antigen molecule. If these antigen molecules are linked 32 CHAPTER 3 by the binding of a second antibody to other epitopes, a cyclic or lattice structure can be formed. The rate of dissociation of any one antibody- epitope binding is the same as for a simple interaction, but because the antigen is still held by other interactions, the overall rate of dissociation is very slow.

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