Abstract
ANALYSES of amino-acid sequences of rabbit, mouse and human immunoglobulins have shed considerable light on the structure and phylogenetic relationships of these molecules1. The heavy and light chains of IgG immunoglobulins each consist of a variable amino terminal half and an invariant carboxyl terminal half. Chemical differences observed in the variable regions of these chains are presumably responsible for the heterogeneity of antibodies present in the total serum gamma globulins. Significant homology in the ammo-acid sequences of light and heavy chains of closely related and distant species has suggested that these polypeptide chains originated by duplication from an ancestral gene coding for a polypeptide chain of about 100 amino-acids2.
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SHUSTER, J., GOODMAN, J. Phylogenetic Studies of Shark Immunoglobulins. Nature 219, 298–299 (1968). https://doi.org/10.1038/219298a0
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DOI: https://doi.org/10.1038/219298a0
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