Abstract
The specificity of bullfrog (BF) (Rana catesbeiana) antibody to rabbit γ globulin (RGG) and hen egg albumin (HEA) was compared to the specificity of mammalian (guinea pig, mouse) antibody to these same proteins. Mammalian anti-RGG was relatively specific whereas BF anti-RGG produced a precipitin reaction with all mammalian sera tested. The BF anti-RGG contained antibody directed to both the Fc and Fab fragments of the RGG, although absorption experiments showed that antibody to the RGG Fc was primarily involved in the cross-reactions. Also, tests with fragments of the heterologous globulins showed that the BF anti-RGG was reacting with the Fc portion of the heterologous globulin. This BF antiserum to RGG detected similar antigenic determinants on the slow γ globulins from other rodents (7Sγ2 of guinea pig, hamster, Peromyscus) and man (IgG), and not on the electrophoretically faster or heavier immunoglobulins of rodents (7Sγ1, IgM) or man (IgA, IgM). A comparison of human IgG subclasses with BF anti-RGG showed that antigenic correspondence was greatest with γG1 and least with γG4. In contrast to the extensive cross-reactivity of BF anti-RGG, BF anti-HEA did not cross-react with other egg albumins (duck, goose) as did guinea pig anti-HEA.

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