Binding of 2,4-dinitrophenyl derivatives by the light chain dimer obtained from immunoglobulin A produced by MOPC-315 mouse myeloma

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Abstract
The L chains, but not the H chains, obtained from IgA produced by the MOPC-315 mouse myeloma bind the 2,4-dinitrophenyl (DNP) group. Specific interaction with the DNP group was determined by using several immunoadsorbents, including DNP-L-lysine-Sepharose, and elution of the adsorbed L chain by DNP-glycine. Equilibrium dialysis experiments showed that the M-315 L chain in the form of a dimer (45,260 daltons) has 2 identical and homogeneous binding sites that bind DNP-L-lysine with an intrinsic association constant of 6.3 .times. 103 M-1. This is the 1st report in which the L chain binding data permit reliable determination of the binding constant and valency of the isolated L chain. A predominant role of the L chain in construction of the binding site in the intact immunoglobulin molecule is suggested.