Abstract
The carboxy terminal portion of Fd of human IgG has been shown to be antigenically similar in all IgG globulins studied. An antibody was made in rabbits against a polypeptide from a myeloma globulin comprising this zone. This antibody was shown to give a reaction of identity with the four subclasses of IgG and other IgG myeloma globulins by precipitation after immunodiffusion. At the same time an antibody made in rabbits against a polypeptide comprising most of Fc as well as commercial anti-IgG showed these IgG globulins to be similarly related. No precipitation with either antibody occurred when several pure alpha and mu chains or either the kappa or the lambda light chains were used as antigens. There was no interaction between the antibody to the Fd and the antibody to the Fc polypeptides. A region in the carboxy half of Fd of IgG antigenically related, and paralleling the constant part of the light chains has therefore been demonstrated by serologic means. This additional constant zone in IgG had been postulated by other investigators.
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Henley, W., Okas, S. & Hodes, H. A zone common to IgC globulins in the Fd region. Pediatr Res 5, 381 (1971). https://doi.org/10.1203/00006450-197108000-00043
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DOI: https://doi.org/10.1203/00006450-197108000-00043