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Abstract
The best criterion for establishing homologies between immunoglobulins from different animal species would certainly be the demonstration of similarities between their amino acid sequences. Such an investigation, although becoming less problematic with the advances in modern protein chemistry, can only be undertaken in a small number of specialized laboratories. It would, however, seem that a valuable substitute for such chemical information is available in the form of immunologic analysis. Serologic cross-reactions between related proteins are known to be due to structural similarities between the antigens and, by extension, to correspondence of their amino acid sequences. There is good justification, therefore, to regard the evidence of clear-cut serologic cross-reactions as a very strong criterion of homology between two polypeptide chains. In the particular case of IgA, the serologic approach has previously been applied only to the identification of IgA in primates (1–7), dogs (8), rats (9) and the pig (Vaerman and Heremans, to be published).

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