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By Ed Harlow and David Lane

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Acad. Sci. 75:2140- 2144. , C. J. Cebra. 1980. gM-bearing B cells and in the normal splenic DNA component of Hybridomas making different isotypes of antibody. Cell 22:349-359. , T. Kawakami, N. Takahashi, and T. Honjo. 1980. Rearrangement of immunoglobulin y 1-chain gene and mechanism for heavy-chain class switch. Proc. Natl. Acad. Sci. 77:919- 923. W. D. Cooper. 1975. Sequential expression of germ line genes in development of immunoglobulin class diversity. Fed. Proc. 34: 33- 39. B. W. J. Harris.

4). This type of multimeric interaction can occur in most immunochemical techniques using secondary reagents. Antigens immobilized on solid supports at high concentrations promote high-avidity, bivalent binding When an antibody binds to an antigen on a solid phase, the interaction is biphasic, and two factors, in addition to the intrinsic affinity, control the strength of the interaction. These are the high local concentration of the antigen and the possibility of bivalent binding. 5 Bivalent binding to antigens immobilized on a solid phase increases the avidity.

The antibody finds the antigen by diffusion. However, the second step of the reaction links the unoccupied combining site of the antibody with an identical epitope on the same antigen molecule. 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 .

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