Abstract
Light polypeptide chains of immunoglobulin G, its fractions obtained upon chromatography in DEAE-Sephadex, as well as purified antibodies to proteins, synthetic polypetides and hapten conjugates of proteins and synthetic polypeptides, were subjected to acrylamide gel electrophoresis. The light chains from all the preparations studied resolved into six to eight distinct bands. Significant differences were found in the electrophoretic mobility of bands from light chains derived from antibodies against antigens with different net charge and from normal rabbit immunoglobulin G fractions which were separated on DEAE-Sphadex. Small differences were also observed in the relative intensities of the bands resolved from light chains of defferent preparations.
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