Abstract
Lactoferrin and IgG were major proteins in whey from involuted bovine mammary glands. Thirty to 50% of the protein with gamma electrophoretic mobility (pH 8.9) was lactoferrin. IgG and lactoferrin were not separated by electrophoresis or filtration through Sephadex G-200. Lactoferrin can be separated from fast-IgG, but not slow-IgG, by ion-exchange chromatography on DEAE Sephadex A-50. Separation of slow-IgG and lactoferrin can be achieved by ion-exchange chromatography on DEAE Sephadex A-50 followed by filtration through Sephadex G-200. These results suggest that lactoferrin, as it exists in whole whey, is in the form of a complex which is broken down by ion-exchange chromatography. While the ratio of fast-IgG to slow-IgG in blood serum is near unity, the concentration of fast-IgG is 3- to 5-fold greater than slow-IgG in the secretion from nonlactating glands. This finding suggests that the mechanism for selective transport of fast-IgG from blood serum to lacteal fluid may be operative in the nonlactating gland.
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