| Abstract: | Carp anti-DNP antibodies were raised by various DNP-carrier conjugates. Their intrinsic affinity (K0) to monovalent E-DNP-L-lysine and functional affinity (DF) for binding to the multivalent DNP-T4 bacteriophages were determined. The functional affinity of antibodies elicited by T-cell-dependent DMPn-HSA (n = 3, 15, 33) is relatively high (KF):1010-1012 M-1). These KF values increase more than K0 during the immune response. The functional affinity is dependent on the molar KNP: HSA ratio. The mediate coupled DMP15-HSA elicits antibodies with the highest functional affinity. Carps immunized with T-cell-independent DNP-conjugates synthesize antibodies which have similar K0 as the antibodies elicited with DNP-HSA. However, the KF-values are in the range from 107 to 1010 M-1 only. The KF of antibodies raised with DNP-BA are 103-104 fold, those of DNP-S III and DNP-Ficoll elicited are only 4 . 101 to 4,7 . 102 fold higher than their corresponding K0-values. This means that these antibodies are not very effective in binding the multivalent DNP-T4. Specifically purified antibodies have also such low functional affinities. These strong differences in the functional affinity of carp DNP-antibodies elicited by T-cell dependent and independent DNP-conjugates are discussed with regard to stimulation of different B-cell subpopulations. |
