Abstract
K-Casein can be separated from [alpha]sl-and [beta]-casein variants as well as from whole casein by diethyl-aminoethyl (DEAE)-cellulose-urea chromatography after reduction of the disulfide bond(s) by 2-mercaptoethanol. k-Casein in the reduced form elutes from DEAE-cellulose at 0.05 MNaCl. The use of a reduction step simplifies purification of the major casein components (a[alpha] sl -, [beta]) by chromatography.