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Journal of Dairy Science Vol. 75 No. 5 1204-1210
© 1992 by American Dairy Science Association ®
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Application of PhastSystem® to the Resolution of Bovine Milk Proteins on Urea-Polyacrylamide Gel Electrophoresis

D. L. Van Hekken 1 and M. P. Thompson 1

1 Agricultural Research Service, USDA, Eastern Regional Research Center, Philadelphia, PA 19118

Optimal conditions were established for alkaline urea-PAGE using modified precast, ultrathin gradient gels on the automated PhastSystem®. Profiles of milk proteins showed that the caseins and whey proteins resolved extremely well. Major bands were observed for alphas1-casein and ß-casein, and alphas2-casein appeared as a well-resolved doublet. In contrast, kappa-casein separated from other caseins as a faint doublet, and purified kappa-casein appeared as one major and one minor band. Whey proteins (serum albumin, alpha-lactalbumin, ß-lactoglobulin) separated into broad bands resolved from each other and from the caseins. Partially (40%) dephosphorylated whole casein showed multiple bands for alphas1-casein and ß-casein at different levels of phosphorylation. Separation of genetic phenotypes was observed for ß-lactoglobulin A and B; alphas1-casein A, B, and C; and ß-casein A, B, and C. Electrophoretic patterns of milk proteins extracted from cheese samples varied among the different types of cheeses. Our modified procedure provides researchers with a rapid technique to separate both caseins and whey proteins on the same urea gel according to their charge to mass ratios.

Key Words: casein • PhastSystem® • urea-electrophoresis • whey proteins

Submitted on September 18, 1991
Accepted on January 6, 1992




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