Recombination of heavy and light chains from human immunoglobulins.

The recombination of reduced, alkylated heavy and light chains from three IgG, two IgM and one IgA pathological protein and from normal IgG has been quantitatively studied. All γ, α and μ chains showed some recombination with all κ and λ chains tested. One of the IgG and two of the IgM proteins showed more than 50 per cent recombination and in these there was evidence of a selective reconstitution of autologous chain pairs; the structural features which determine re-association appear to be independent of the electrophoretic mobility, or antigenic and allotypic specificity of the interacting chains. The chains of normal IgG and of three myeloma proteins showed a low percentage recombination and these autologous chain pairs did not combine preferentially. It appears that immunoglobulin chains show a variable ability to regain their native configuration after isolation. Two pathological κ chains which were identical in electrophoretic mobility and Inv specificity but not equivalent in re-association behaviour showed well marked differences in tryptic peptide patterns. This indicates that the number of chemically distinct human light chains exceeds the forty variants previously postulated on the basis of antigenic, allotypic and electrophoretic differences.