Light Chain Types in Pig Antibodies to the 2,4‐Dinitrophenyl Group

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Abstract
Sera of individual pigs immunized by dinitrophenylated bovine immunoglobulin served as the source of antibodies to the 2,4‐dinitrophenyl group and of γG‐immunoglobulin isolated after absorption of antibody (nonspecific γG‐immunoglobulin). The S‐sulfo‐derivatives of light chains of antibody and of nonspecific immunoglobulin were separated by ion‐exchange chromatography on SE‐Sephadex into the individual types (λ‐, π‐ and ϱ‐chains). Fingerprinting as well as immunoprecipitation failed to reveal any differences between the corresponding types of light chains of antibodies and of nonspecific immunoglobulin. In comparison with nonspecific immunoglobulin of normal animals the ratio of the individual types was shifted in favour of the π‐ and ϱ‐chains both with antibodies and with nonspecific immunoglobulin of immunized animals. As shown by peptide map analysis, the ϱ‐chains are in certain respects related to the heavy chains. They contain hexosamines and their amino acid composition is different from that of the γ‐ and ϱ‐chains. The data on weight ratio of heavy to light chains in the antibodies support the conclusion that the major component of the ϱ‐chains is not represented by heavy chain fragment but by a separate type of light chains.