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Fractionation of Caseins Directly from Skimmilk by Gel Chromatography. 2. Elution with Phosphate Buffers¹

Department of Food Science, University of British Columbia, Vancouver 8, Canada

ABSTRACT

-Casein was separated on Sephadex G-100 by eluting with 0.01 M borate, pH 10 at 25 C or 0.01 M phosphate, pH 11 at 4 C. Phosphate, 5 mM with 2 mM Na ethylenediaminetetraacetate, pH 10.8, was used for continuous fractionation at 4 C to retard bacterial growth in the gel. -Casein was collected from the first half of the first peak. The stabilizing ability of the -casein against Ca-±_sl-caseinate precipitation was slightly low possibly from contamination with minor members of the ±_s-casein group. Eleetrophoretically pure ²-casein was obtained from the first half of the second peak after elimination of contaminating ±_s-casein by precipitation at pH 4.4 and 4 C. ±_s-Casein was purified from the last half of the second peak by precipitating with 0.1 M CaCl₂. The phosphate method was superior to the sodium dodecylsulfate method because of faster elution, being more reproducible, and without extraction to remove bound dodecylsulfate. ±_s-, ²-, -Caseins were fractionated directly from skimmilk, however, the yield of -casein was approximately half of that by the sodium dodecylsulfate method.

¹ Supported by Operating Grant 0012 of the Canada Department of Agriculture, Ottawa.