Studies on the Specificity and Affinity of α, DNP-Oligolysine Antibody: A Basis for Questioning the Role of Cell-Bound Antibody in Cellular Recognition of Antigen

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Abstract
The specificity and affinity of serum antibody made to α, DNP-oligolysines was investigated by equilibrium dialysis, fluorescence quenching and inhibition of precipitation. The combining site of this antibody was found to have an upper limit in size complementary to α, DNP-Lys7. The increase in binding energy of α, DNP-Lys7 over α, DNP-Lys5–6 was found to be a relatively small fraction of the total binding energy. These results are contrasted to those of previous studies which showed that both immunologically competent or committed cells can readily distinguish between α, DNP-Lys5–6 and α, DNP-Lys7. The difference in specificity between the antibody-binding site and the proposed cellular receptor suggests that cell-bound antibody of the conventional type is not the mediator of antigen recognition by cells.

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