Studies on the chemical basis of the antigenicity of proteins. 3. The role of rigidity in the antigenicity of polypeptidyl gelatins

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Abstract
Poiy-L-cyclohexylalanyl gelatins are relatively powerful antigens, as followed by the precipitin reaction. The antibodies to the 2 antigens investigated could be also cross-precipitated by other polycyclohexylalanyl derivatives. The attachment of serine did not convert gelatin into a more powerful antigen. Antibodies to poly-L-seryl gelatin could not be detected by the usual precipitin techniques, but their presence could be shown by a method similar to that used by Maurer (1954) to demonstrate the antigenicity of gelatin. In view of the increase in antigenicity as a result of the attachment of aromatic amino acids, cyclohexylalanine or cysteine to gelatin, it was concluded that areas of rigidity in the molecule are a necessary prerequisite for the enhancement of the antigenicity of gelatin. The use of some synthetic polypeptides containing proline or hydroxyproline or both in inhibition experiments, intended to detect the chemical nature of the antigenically active sites of gelatin, was unsuccessful. Various polypeptidyl gelatins were caused to cross-react with the antiserum to gelatin. An increase in the amount of the amino acid attached to gelatin diminished considerably the extent of precipitation.

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