In competitive recombination experiments using non-alkylated heterologous H and L chains of monotypic immunoglobulins of different classes, subclasses and VL subgroups, an order of sequence in preferential reassociation of chains was proved. Preferential association on class and subclass level was found when H and L chains obtained from proteins of different classes and subclasses were used. The influence of the VL subgroup property was only found, when the chains were derived from proteins of identical subclasses. There was no significant difference between the attachment to H chains of autologous and heterologous L chains of identical subgroups. The influence of the exchange of L chains with heterologous L chains of different subgroups on the antibody activity of IgMK cold-agglutinins was also controlled. Molecules containing μ chains of IgMK cold-agglutinins and heterologous L chains agglutinated erythrocytes at +4°C. The fixation of isolated μ chains of IgMK cold-agglutinin antibodies to erythrocytes at +4°C was also demonstrated. The importance of the folded structure in preferential association of immunoglobulin polypeptide chains and significance of the overall conformation of the immunoglobulin molecules in antibody activity is discussed.
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