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 αs1-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 αs-casein was separated from acid casein on Sephadex G-100 by eluting with 0.5 HIM sodium dodecylsulfate. κ-Casein stabilized this αs1-casein against Ca++ to the same extent as the αs1-casein prepared by the method of Zittle and Custer.
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