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  • Author or Editor: Susan H. Socher x
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Summary

Antisera raised in rabbits against either purified recombinant-derived human tumor necrosis factor (tnf)- α (hutnf) or hutnf peptide-bovine thyroglobulin conjugates were evaluated for anti-equine tnf (eqtnf) activity. Binding and neutralizing anti-eqtnf activities were found in antisera raised against whole hutnf or against either of the peptides containing the N-terminal 15 amino acids of hutnf (hutnf[1-15] and hutnf[1-31]). Anti-eqtnf activity was not detected in antisera raised against hutnf[65-79], hutnf[98-111] or hutnf[124-141] peptides. The addition of excess hutnf[1-15] completely inhibited the ability of anti-hutnf[1-15] to bind eqtnf and reduced by approximately 25% the anti-eqtnf activity of an antiserum raised against whole hutnf. Nonconjugated hutnf[1-15] did not have eqtnf agonist or antagonist activity. Results were consistent with previous structural and functional data implicating the N-terminus of hutnf in receptor binding and indicate that the homologue of hutnf[1-15] on eqtnf may be a potentially important target for neutralizing anti-eqtnf antibodies.

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in American Journal of Veterinary Research