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

[摘要] 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 ε-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.

[学科分类] 生物科学（综合）