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  • Title: Studies on Xenopus laevis immunoglobulins.
    Author: Hadji-Azimi I.
    Journal: Immunology; 1971 Sep; 21(3):463-73. PubMed ID: 4105472.
    Abstract:
    The anuran amphibian Xenopus laevis has been shown to produce two classes of antibodies to HGG, BSA and Hc. These antibodies were characterized by gel filtration on Sephadex G-200 as `19S' and `7S' immunoglobulins. In the course of immunization, antibody activity could be initially detected in the `19S' immunoglobulin fraction, followed by the appearance of the activity in the `7S' immunoglobulin fraction at a later stage of immunization. A switch-over from `19S' to `7S' activity was not observed. Both immunoglobulins were composed of heavy and light polypeptide chains. The `19S' protein had heavy chains with a molecular weight of 74,500, similar to human μ-chain (73,900). The `7S' protein differed from human IgG in respect to the molecular weight of its heavy chain which was shown to be 64,500. Light chains of both immunoglobulins of Xenopus were found to have a molecular weight of 26,700, similar to human immunoglobulin light chains (25,000).
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