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Heterogeneity in the Complementation of Polypeptide Subunits of a Purified Antibody Isolated from an Individual Rabbit¹

From the Department of Microbiology, University of Illinois, Urbana, Illinois

Abstract

Experiments on complementation were carried out with light and heavy chains of antidinitrophenyl antibodies, purified from the serum of the same rabbit but differing in affinity for the hapten. Light chains derived from antibody of higher affinity were more effective than the light chains of low affinity antibody in complementation with their homologous heavy chains, but were equally or less effective when combined with the heavy chains of the antibody of lower affinity. The results indicate heterogeneity of the light chain population with respect to their effectiveness in complementation. A similar conclusion was reached with respect to the population of heavy chains. The data suggest that different clones of cells utilize different pairs of polypeptide chains in the synthesis of antibody of a given specificity.

Footnotes

¹ Supported by Grants AI-06281 and AI-05252 from the National Institutes of Health and GB-1563 from the National Science Foundation.

² This work was carried out during the tenure of a Career Development Award (R. H.) and a Research Career Award (A. N.) from the National Institutes of Health.

Dr. Hong's present address: Department of Pediatrics, University of Minnesota School of Medicine, Minneapolis, Minnesota.