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Electrophoretic, Immunoelectrophoretic, and Ultracentrifugal Characterization of Proteins in Whey Fractions Prepared by Salt Fractionation¹

Department of Food Science and Nutrition, The Ohio State University, Columbus 43210

ABSTRACT

Polyacrylamide gel disc electrophoresis (PAGE) in alkaline and acid buffers, immunoelectrophoresis, analytical ultracentrifugation, and sucrose density gradient were used to isolate immunoglobulins from bovine milk and colostrum by ammonium sulfate fractionation. The immunoglobulins were relatively free of other whey proteins and moved as one component on PAGE at pH 9.5. However, on PAGE at pH 4.3, one major and two minor components were evident. By analytical ultracentrifugation, immunoglobulins from colostrum of one cow resolved into three peaks with coefficients of 6.4S, 10.6S, and 18.8S for a second cow, only two peaks at 6.5S and 19.0S were present. Components corresponding to these coefficients were separated by linear density gradient in 10 to 40% sucrose.

¹ Article 10:71. Department of Food Science and Nutrition. This investigation was supported by Public Health Services Grant FD-00161 from the Office of Research and Training Grants, Food and Drug Administration.