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Heterologous Recombination between Mouse Myeloma 315 Heavy Chains and Rabbit Antibody Light Chains: Structural and Functional Properties of the Hybrid Molecules¹

From the Department of Medicine, The Jewish Hospital of St. Louis and the Departments of Medicine and Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110

Abstract

7S recombinant molecules have been obtained from the heavy (H) chains of mouse myeloma protein 315 (which binds 2,4 dinitrophenyl (DNP) ligands) and the light (L) chains from rabbit anti-DNP antibodies or normal rabbit IgG. H- and L-chain antigenic determinants were detectable on these recombinants, and they displayed structural properties that closely resembled those of the parent molecules with respect to sedimentation coefficient, H- to L-chain ratio, and gel filtration characteristics. Recombinants containing L-chains from anti-DNP antibodies showed significantly greater binding of -DNP-lysine than hybrids made with nonspecific L-chains. Idiotypic determinants characteristic of the intact protein 315 were not recovered on any of these recombinants to any greater extent than were expressed on 315 H-chains alone. These results indicate that a DNP-binding site structure can be obtained by interaction between immunoglobulin subunits from different species, provided that they originate from anti-DNP molecules. Also, these data indicate that monoclonal H-chains reconstituted with polyclonal L-chains display binding properties resembling a polyclonal (heterogeneous) antibody population.

Footnotes

¹ This work was supported, in part, by Research Grant AI09723 from the National Institute of Allergy and Infectious Diseases, and Research Grant NP-110A from the American Cancer Society.

² Recipient of a fellowship from the Swiss National Fund for Scientific Research.

³ Recipient of a Research Career Program Award (AM-38,620) from the National Institute of Arthritis and Metabolic Diseases.

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