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An Electrophoretic Study of the Protein in Skimmilk¹

Departments of Dairy Technology and Chemistry, The Ohio State University, Columbus

ABSTRACT

The physical and chemical properties of milk proteins have been studied by many investigators. In most cases the milk proteins were isolated by chemical methods and studied as separate entities, and there is some question as to whether these separated proteins exhibit the same characteristics as they do in their natural state in milk. Therefore, it was the purpose of this investigation to study the electrophoretic properties of the proteins of unfractionated bovine skimmilk over a range of pH 's and ionic strengths and to compare the observed properties with those reported for the isolated components. In addition, a limited study of the effect of heat treatment on the unfractionated proteins of skimmilk was undertaken to demonstrate the possibilities of electrophoretic analyses as applied to unfractionated protein systems.

Mellander (8) examined unfractionated bovine skimmilk in a Tiselius electrophoresis apparatus at pH 6.9 and ionic strength 0.1 and reported the presence of four components, which he named -casein, lactalbumin, ß-casein, and -casein in the order of decreasing mobility.

¹ Article no. 3-52, Department of Dairy Technology, The Ohio State University. Financed in part by the Ohio Dairy Products Research Fund.