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Isolation, Purification, and Determination of Some Chemical and Physicochemical Characteristics of Sheep Alpha_s-Casein

Institute of Animal Breeding, Department of Milk Biology, Sofia, Kostinbrod, Bulgaria

ABSTRACT

Alpha_s-casein was isolated from whole casein by precipitation with 6.6 M urea. The precipitate revealed contamination with ß-casein when it was characterized by starch-gel electrophoresis. Purification was effected by three treatments on a Sephadex G-150 column. The sample (up to 1.0 g protein for each) and Sephadex were equilibrated with .005 M Tris-citrate buffer, pH 8.6, containing 6 M urea. Elution was performed with the same buffer at 21 to 25 C. The final preparation was sufficiently pure by starch-gel electrophoresis. Sheep _s-casein's molecular weight is 47,500, diffusion constant D°²⁰ –7.21, and Stake's radius 29.65. Absorbance at 280 nm A^1cm_1% is 8.45. Sheep _s-casein's spectrum revealed maximum absorbance at 278 nm.