Variation in the Size of Antibody Sites for the Poly-l-Aspartate Hapten during the Immune Response

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Abstract
Rabbit antisera specific for poly-l-aspartate were prepared by immunization with poly-l-aspartyl-bovine serum albumin. Homogeneous l-aspartate oligopeptides were isolated from partially acid hydrolyzed commercial poly-l-aspartic acid by DEAE-cellulose chromatography. Hapten inhibition of the anti-poly-l-aspartylbovine serum albumin-poly-l-aspartyl-rabbit serum albumin reaction by l-aspartate oligomers was studied in a single rabbit with sera isolated after the first and second immunizations. The ability of oligopeptides to inhibit the poly-l-aspartate immune system increased with the size of the oligopeptide. With first course antisera an upper limit was reached with the triaspartate. With second course antisera the upper size limit of antibody-combining sites appeared to be larger than that found early in immunization.

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