Preferential homologous recombination of H and L chains from mouse myeloma proteins which bind DNP ligands.

Abstract Homologous chain recombinants are formed preferentially when the heavy chains of the murine myeloma proteins 315 and 460 are placed in competition with a mixture of the light chains of both proteins during renaturation and recombination. Both the molar ratio of homologous to heterologous light chains and the high specific binding to DNP-lysine-sepharose demonstrate this preference. It is suggested that the small magnitude of the preference may correlate with the similarity of the 315 and 460 proteins with respect to binding specificity.