Purification of αS1-Casein by Fast Protein Liquid Chromatography

Abstract
An enriched .alpha.S1-casein was prepared by batch fractionation of whole casein on DEAE-cellulose using CaCl2 as eluent. The .alpha.s1-casein fraction was then submitted to hydrophobic interaction chromtography on a semipreparative fast protein liquid chromatography system. Electrophoretically pure .alpha.s1-casein was obtained by eluting with .05 M sodium phosphate at pH and containing 3.75 M urea.