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- W2034403162 abstract "Abstract κ-Casein was isolated directly from skimmilk without separating acid casein for application to a Sephadex G-100 column by eluting with 1.5mM sodium dodecylsulfate at 4C. The separated κ-casem contained bound dodecylsulfate and revealed decreased stabilizing ability, approximately 70%, against α s1 -casein in the presence of Ca ++ . Partial elimination of bound dodecylsulfate by dialysis in urea and 2-mercaptoethanol restored most of the stabilizing ability of κ-casein. However, no simple method for removing the dodecylsulfate completely was found except acetone extraction which aggregated κ-casein with decreased stabilizing ability. Eleetrophoretically pure α s -casein was separated from acid casein on Sephadex G-100 by eluting with 0.5 HIM sodium dodecylsulfate. κ-Casein stabilized this α s1 -casein against Ca ++ to the same extent as the α s1 -casein prepared by the method of Zittle and Custer." @default.
- W2034403162 created "2016-06-24" @default.
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- W2034403162 date "1972-01-01" @default.
- W2034403162 modified "2023-09-29" @default.
- W2034403162 title "Fractionation of Caseins Directly from Skimmilk by Gel Chromatography. 1. Elution with Sodium Dodecysulfate" @default.
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- W2034403162 doi "https://doi.org/10.3168/jds.s0022-0302(72)85426-2" @default.
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