Search

Three day cultures of human peripheral blood lymphocytes (PBL) contain significant numbers of lymphoblasts binding 125I-alpha 1-AT as well as those with membrane-associated alpha 1-AT detectable by immunofluorescence. Co-cultivation of PBL with T cell mitogens leads to the appearance of lymphoblasts with membrane-associated alpha 1-AT while B cell mitogens induce lymphoblasts with a binding capacity for 125I-alpha 1-AT. It could be shown that unstimulated lymphocytes neither have membrane-associated alpha 1-AT nor possess a binding capacity for it. The highest number of lymphoblasts with membrane-associated alpha 1-AT was found in Con A stimulated cultures as revealed by indirect immunofluorescence. By contrast, PHA or PPD stimulated cultures contained much less such cells of lower fluorescence intensity. Co-cultivation of PBL with the B cell mitogens LPS and rabbit-anti-human gammaglobulin-IgG-F(ab')2 induced lymphoblasts with a clear binding capacity for 125I-alpha 1-AT, while dextran-sulphate had no effect. A possible regulative role of alpha 1-AT in the immune response is discussed.

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.

Carp IgM as well as carp anti-DNP-antibodies migrate electrophoretically very well as a diffuse band into polyacrylamide gel of large pore size. The isoelectric spectra of the carp anti-DNP-antibodies are heterogeneous and show bands in the pI-range of 4.0 to 6.4. The activity of focused anti-DNP-antibodies could be demonstrated in the pI range between 5.4 to 6.4 even in high antibody dilutions. The investigated structural heterogeneity of the anti-DNP-antibodies of carp is a further proof for the phylogenetically early onset of a large antibody heterogeneity of lower vertebrates.