Abstract
Cellulose acetate electrophoresis and PAGE techniques were compared for fractionation and quantification of milk proteins. Protein bands were stained with Ponceau-S and aniline blue black in the cellulose acetate electrophoresis and PAGE, respectively. αs1-Casein and β-casein absorbed almost equal quantities of Ponceau-S per unit weight, whereas β-casein absorbed more aniline blue black per unit than did αs1-casein. β-Lactoglobulin, α-lactalbumin, and bovine serum albumin absorbed equal amounts of Ponceau-S per unit but differed in absorption of aniline blue black. It was concluded that cellulose acetate electrophoresis was the method of choice for rapid fractionation and quantification of milk proteins.
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