Purified, iodinated bovine immunoglobulins (Igs) were incubated with fresh Guernsey milk or with the casein, fat and whey fraction of such milk for up to 12 hr at 37°C. Igs incubated in whole milk, showed little evidence of proteolysis in either the whey, fat or casein fractions although the amount of radioactivity which became associated with the latter two fractions prevented adequate analysis. When the individual milk fractions were first prepared and then incubated with iodinated Igs, we found no evidence for proteolysis of any Ig in whey or casein but ca. 25% breakdown or dissociation of the IgM and SIgA which had been incubated with milk fat. Breakdown of these Igs in fat was not inhibited with benzamidine-HCl, sodium azide or EDTA. These data show that: (i) only those Igs which associate with milk fat are degraded or dissociated by it and (ii) the Ig fragments described from cows milk or recovered during studies on Ig transport cannot be ascribed to the proteolytic activity of fresh milk.
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