MOPC 104E IgM/anti-idiotype solid-phase inhibition assay as a model for screening myeloma proteins for ligand binding specificity.

The inhibition of binding of 125I-labeled MOPC 104E IgM anti-idiotype to the controlled pore glass-bound IgM by various oligo- and polysaccharides was investigated as a model for the screening of myeloma proteins with unknown hapten binding specificity. The inhibitory efficiencies of the different haptens in this system were found to correlate well with their known abilities to bind to MOPC 104E IgM. Thus B1355S dextran, nigerosyl-alpha (1-3)-nigerose, and nigerosyl-alpha (1-3)-glucose, all known for specific binding to MOPC 104E IgM, were efficient inhibitors in the assay, in contrast to a series of more or less unrelated carbohydrate compounds, which showed only weak inhibitory capacity. According to these results there seems to be no obstacle to applying the anti-idiotype assay system to screening myeloma proteins whose binding specificity has not yet been determined.