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Starch Gel Electrophoresis of Various Fractions of Casein

Division of Applied Biology, National Research Council, Ottawa, Canada

ABSTRACT

Preparations of -, ß-, -, -, and -caseins were compared by electrophoresis in starch gel and in free solution. Acid casein separated into at least 17 zones. All fractions of casein contained numerous proteins, but the preparatory procedures brought about considerable enrichment of certain zones while weakening or eliminating others, and a tentative identification of specific zones with each casein fraction was, therefore, possible. _s-Casein appeared to be contaminated with traces of ß-, -, and -casein, but the main contaminants were unidentified fractions travelling between _s- and ß-casein. ß-Casein was contaminated with traces of - and -casein, and with the unidentified fractions observed in _s-casein. Our preparations of -casein were heavily contaminated with - and ß-casein, and contained lesser amounts of _s-casein and of unidentified fractions. Identification of the -casein zone was confirmed by zone electrophoresis from urea solution into urea-free gel, whereupon the -casein formed a characteristic precipitation zone, and by electrophoresis in gels containing calcium. Comparison of three -casein preparations indicated differences among them, both in stabilizing power and in electrophoretic properties. The preparation of -casein with the least contamination from other casein components appeared to be partially denatured.