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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