Abstract

DURING the past few years our knowledge of the immunoglobulins of man and mammals has been substantially extended. The method of making antiglobulin sera developed by Milgrom et al. in 1956 (ref. 1) has played a decisive part in this particular connexion. As is well known, this method makes it possible to prepare antisera which react, in addition to γ-globulins (IgG, IgA, IgM), with complemental factors, if any2. Since our knowledge of non-mammalian immunoglobulins is limited3–10, I prepared (using a modification of Milgrom's method2) antisera to the globulins of mammals (horse, cattle, hog), birds (duck, goose), turtles (Testudo hermanni Gmelin), and fishes (Cyprinus carpio L., Tinca tinca (L.), Perca fluviatilis L., and Ictalurus nebulosus Le Sueur). The serum concentration used to bring about coupling with erythrocytes was chosen so that, for the mammals, only antibodies were detectable against the γ-globulins during immunoelectrophoresis. In this connexion, distinct precipitate lines of the IgG and IgM globulins were always observed. Moreover, for both horse and hog a weak line was observed corresponding to the IgA globulin. The antisera prepared against the globulins of goose and duck showed wide identity during immunoelectrophoresis. Two parallel lines were found that could be assigned to the IgG and IgM globulins (Fig. 1A). Clearly visible is a splitting up of the IgG line in the anodic region.

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