Preparation of κ-Casein by Gel Filtration

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Abstract
A procedure for the preparation of pure K-casein by Sephadex gel filtration is described. Unreduced casein is filtered through a 2.5-by 95-em colmnn of Sephadex G-150 equilibrated with 0.005 ~ triscitrate buffer, pit 8.6, containing 6 urea. K-Casein is excluded from the gel and emerges as a sharp peak at the void volume; all other caseins are retarded by the gel. The method is particularly suitable for preparing pure Kicasein in good yield from small quantities of whole casein, but larger amounts of n-casein are readily prepared. The method is also suitable for the purification of K-casein-rich preparations.

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