Electrophoretic Heterogeneity of Polypeptide Chains of Specific Antibodies

Abstract
Heavy and light polypeptide chains isolated from different specific antibodies to haptens and from γG-immunoglobulin of normal rabbits have been resolved into distinct, multiple components by disc electrophoresis in polyacrylamide gels in the presence of urea. In spite of the resolution of these chains into multiple bands, different specific antibodies and normal rabbit γG-immunoglobulin were indistinguishable from each other by this method.