A milk immunoglobulin concentrate (MIC) containing antibodies to enteropathogenic E. coli strains was prepared by hyperimmunisation of pregnant cows and using the milk obtained during the first 6 to 8 days of lactation. The sterile concentrate contained 70 to 80% protein and 35 to 40% immunoglobulin. The antibacterial activity was measured by bacterial passive agglutination, bacteriostatic activity in vitro, phagocytic clearance in vivo, and a protection test in mice. Though differences in titers were observed, adequate immunologic activity was demonstrated by these tests. Clinical studies were performed with 60 patients (aged 10 days to 18 months) suffering from diarrhoea with isolation of enteropathogenic E. coli. They were treated for 10 days with MIC and stool cultures were done prior to, during, and 2, 3 and 4 days after termination of treatment. Among 51 patients infected with E. coli strains incorporated in the vaccine, stool cultures became negative in 43 (84.3%) after treatment with MIC and 8 remained positive. Nine patients infected with strains O 78:K80(B-) and O 114:K--(B-)--which were not included in the vaccine used for immunisation--served as controls. Only one patient in this group became negative. If all patients receiving antibiotics for non intestinal infections during the treatment period are omitted the results remained unaltered: MIC was effective in 32 out of 38 patients (84.2%). These differences were highly significant. These results provide evidence that treatment with specific MIC is effective in eliminating enteropathogenic E. coli from the intestine.

beta-Conglycinin (7 S globulin) and glycinin (11 S globulin) are the major reserve proteins of soybean. They were localized by the protein A immunogold method in thin sections of Glycine max (soybean) cv. Maple Arrow. In cotyledons, both globulins were simultaneously present in all protein bodies. Statistical analysis of marking intensities indicated no correlation between globulin concentration and size of protein bodies. The immunogold method failed to detect either globulin in the embryonic axis and in cotyledons of four-day-old seedlings. Similar observations were made with cotyledons of two soy varieties lacking either the lectin or the Kunitz trypsin inhibitor. In another variety (T-102) lacking the lectin, the 7 S globulin could not be detected.

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A complete secretory immunologic system has been identified in the equine species. It is characterised by the presence of a secretory component either bound to secretory IgA (SIgA) or remaining in the free form (FSC). The mean molecular weights of SIgA, serum IgA and FSC have been estimated. The homology of the equine and human IgA classes have been demonstrated by cross-reaction with anti-human IgA antisera. A quantitative study of equine immunoglobulins in various fluids have shown that SIgA is predominant in saliva, mature milk, nasal and lacrimal secretions, but not in colostrum. In vitro binding of human and bovine FSC is found to occur mostly with the polymeric form of equine serum IgA.

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