Abstract
The major species of antibody present in the rat external secretions, saliva and colostrum was found to be an intermediate sedimenting (approximately 11 S) immunoglobulin of rapid mobility apparently analogous to human IgA. Antibody activity was demostrated by radioimmunoelectrophoresis of colostrum obtained following intramammary injection of bovine serum albumin. Using antisera prepared against partially isolated secretory IgA, serum IgA could be demostrated. IgA was present in small amounts in serum, and was primarily 7S in sedimentation although higher polymers (17 S) were also detected by gel filtration. Serum IgA was significantly more rapid (anodal) in electrophoretic mobility than secretory IgA, and this was not dependent on differences in sialic acid content.
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