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Lactoferrin and IgG Immunoglobulins from Involuted Bovine Mammary Glands

Department of Dairy Science, Ohio Agricultural Research and Development Center, Wooster 44691

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.