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The basic four-chain model for the immunoglobulins originally proposed by Porter' has been confirmed by subsequent studies.2 Mild reduction of IgG3 at neutral pH, followed by gel filtration in suitable dissociating solvents, results in separation of the heavy (H) and light (L) polypeptide chains.4 It has been demonstrated repeatedly that separated chains can be recombined, and that the product has hydrodynamic properties essentially similar to the original IgG molecule.5 Hybrid recombination between heavy and light chains from a chemically and functionally heterogeneous population of IgG molecules (even from different species) can be easily achieved.5 However, Mannik6 has recently shown, using human IgG myeloma proteins, that H chains preferentially recombine with the L chains with which they were previously associated, even in the presence of an excess of L chains from another source. When IgG molecules with specific antibody activity have been studied, recombination of heavy and light chains have yielded a product capable of combining with the specific antigen.7-1" Higher recovery of activity followed recombination of specific H chain with specific L chain than with nonspecific L chains.8 9, 11-16 These findings strongly suggest that full recovery of the binding site conformation requires correct pairing of constituent polypeptide chains. The optical rotatory dispersion studies described below give physical confirmation of this specificity requirement.

Conformational change and complementarity in the combination of H and L chains of immunoglobulin-G.