Comparison of variable region primary structures within an anti-fluorescein idiotype family.

摘要: Abstract Previous reports described the properties of a high affinity (Ka = 1.7 X 10(10) M-1) prototype anti-fluorescein monoclonal antibody 4-4-20, an intermediate 3.7 10(7) 9-40, and Ig members 9-40 idiotype family (comprised 3-24, 5-14, 5-27, 10-25 12-40). Although seven antibodies expressed similar active site structural determinants (idiotypes) as determined serologically, each was characterized by different affinities for fluorescein fine specificity binding patterns. Partial heavy (H)- light (L)-chain N-terminal amino acid sequence analyses revealed all (except 5-27) were composed highly homologous VHIII(C) V kappa II subgroup genes, respectively. Antibody 5-27 utilized VHIII(B) genes shared low V-region homology with remaining family. In addition, complete VH- VL-region primary structures to better understand antibody-antigen interactions. 4-4-20 VH-gene, truncated Sp2 D gene segment, JH4, VL-gene, J 1. VH VL complementarity-determining regions contained many basic aromatic residues capable interaction fluorescein. Results are discussed in terms idiotypic fluorescein-binding characteristics well functional diversity immune response.