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- W2059958725 abstract "Abstract κ-Casein was separated on Sephadex G-100 by eluting with 0.01M borate, pH 10 at 25C or 0.01M phosphate, pH 11 at 4C. Phosphate, 5mM with 2mM Na ethylenediaminetetraacetate, pH 10.8, was used for continuous fractionation at 4C to retard bacterial growth in the gel. κ-Casein was collected from the first half of the first peak. The stabilizing ability of the κ-casein against Ca-α sl -caseinate precipitation was slightly low possibly from contamination with minor members of the α s -casein group. Eleetrophoretically pure ²-casein was obtained from the first half of the second peak after elimination of contaminating α s -casein by precipitation at pH 4.4 and 4C. α s -Casein was purified from the last half of the second peak by precipitating with 0.1M CaCl 2 . The phosphate method was superior to the sodium dodecylsulfate method because of faster elution, being more reproducible, and without extraction to remove bound dodecylsulfate. α s -, ²-, κ-Caseins were fractionated directly from skimmilk, however, the yield of κ-casein was approximately half of that by the sodium dodecylsulfate method." @default.
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- W2059958725 date "1972-01-01" @default.
- W2059958725 modified "2023-09-28" @default.
- W2059958725 title "Fractionation of Caseins Directly from Skimmilk by Gel Chromatography. 2. Elution with Phosphate Buffers" @default.
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- W2059958725 doi "https://doi.org/10.3168/jds.s0022-0302(72)85427-4" @default.
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