Identification of different antigenic determinants within the synthetic multichain Co-polymer poly(LTyr,LGlu)-poly(DLAla) -- poly (LLys), (T,G)-A--L, as recognized by the chicken. II. Fine-specificities of the anti-(T,G) part of chicken anti-(T,G)-A--L antisera
- PMID: 82272
- DOI: 10.1111/j.1365-3083.1978.tb00523.x
Identification of different antigenic determinants within the synthetic multichain Co-polymer poly(LTyr,LGlu)-poly(DLAla) -- poly (LLys), (T,G)-A--L, as recognized by the chicken. II. Fine-specificities of the anti-(T,G) part of chicken anti-(T,G)-A--L antisera
Abstract
Sera from three chickens obtained from a genetic high-responder inbred strain immunized with the multichain polypeptide poly(LTyr,LGlu)-poly-(DLAla)--poly(LLys) (T,G)-A--L) were analysed for possible restrictions in the fine-specificities of anti-(LTyr,LGlu) antibodies. A panel of synthetic hexa- and heptapeptides composed of L-Tyr and L-Glu residues linked to a C-terminal spacer tripeptide, and with L-Tyr as N-terminal, were used as inhibitors in a double-antibody radioimmunoassay. Results showed that all peptides tested possessed some inhibitional potential, although the percentage of displacement for the different sequences varied between 43% and 58%,20% and 56%, and 48% and 85%, respectively, for the three sera tested at a given inhibitor concentration. Different peptide sequences appeared as the most efficient inhibitor in the three sera tested. No simple relationship was found between substitution/elongation of inhibitor peptides and their inhibitional potential, as would have been expected from a simple conception of (T,G)-A--L possessing only one sequential determinant. Possible evidence for conformational determinants in the (T,G)-A--L antigen is discussed.
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