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Effect of Method of Preparing Iso-Electric Casein on Its Electrophoretic Properties ¹

Department of Dairy and Food Industry, Iowa State University, Ames

ABSTRACT

Variations in the method of preparing and purifying iso-electric casein have a significant effect on its electrophoretic properties. Peptization of casein with sodium hydroxide, even at pH 7.0, removes -casein in the subsequent washing. This explains the absence of -casein from some electrophoretic patterns reported in the literature.

Beta- and -casein were removed by washing, only when the casein had been treated with sodium hydroxide. However, the pH of the wash water has a significant effect on the relative percentage composition of -, ß-, and -casein and on their electrophoretic mobilities.

Standardization of the methods for preparation and purification of iso-electric casein are needed if the data reported by investigators are to be compared.

¹ Journal paper No. J-4587 of the Iowa Agriculture and Home Economics Experiment Station, Ames, Iowa. Project No. 1298.

² Present address: Dairy and Food Science, Department of Animal Science and Range Management, Montana State College, Bozeman, Montana.