Purification of αS1-Casein by Fast Protein Liquid Chromatography

Abstract An enriched α S1 -casein was prepared by batch fractionation of whole casein on DEAE-cellulose using CaCl 2 as eluent. The α S1 -casein fraction was then submitted to hydrophobic interaction chromatography on a semipreparative fast protein liquid chromatography system. Electrophoretically pure α S1 -casein was obtained by eluting with .05 M sodium phosphate at pH 6 and containing 3.75 M urea.