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Studies on synthetic polypeptide antigens. XIII. The effects of systematic variation in composition and chemical modifications of the synthetic polypeptides on the antibody-synthetic polypeptide antigen interaction



Studies on synthetic polypeptide antigens. XIII. The effects of systematic variation in composition and chemical modifications of the synthetic polypeptides on the antibody-synthetic polypeptide antigen interaction



J Biol Chem 239(9): 3083-3092



A series of polymer? containing glutamic acid and lysine in varying amounts has been studied chemically and immunologically in rabbits. All of the polymers were approximately the same size and titrated normally with the exception of poly Glu42Lys5, which had an adnormally high acidic pKj, an abnormally low basic pKi( and high interaction parameters for both glutamic acid and lysine. The immunochemical studies with this series of polymers and their various modifications indicated that lysine played a more important part in the antigenic sites of polymers containing both glutamic acid and lystine than did glutamic acid. This conclusion was consistent with the findings of previous inhibition studies. The chemical modifications of poly Glu59Lys41 produced marked changes in the antigenic specificity. Guanidinated lysine was a very strong antigenic determinant, acetylated lysine and methyl esterified glutamic acid were strong determinants, and deami-nated lysine was a relatively nonspecific and variable determinant. Succinylation of poly Glu59Lys4l rendered the polymer incapable of eliciting an antibody response and of cross-reacting with antisera to various glutamic acid-lysine containing polymers; it is essentially equivalent to poly Glu.

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