Affinity Chromatography of Ovine Casein

Abstract

Sheep milk casein was separated into two fractions: one containing <Xsl-plus 13and the other <Xs2 plus K-caseins by a.ftmity chromatography on activated thiol-Sepharose 4B. Milk samples were from the Leccese breed with the most common electrophoretic pattern. Electrophoresis of the chromatographic fractions on SDS-PAGE and on starch urea gel at pH 8.6 and 1.7 clarified the electrophoretic pattern of whole casein. Acidic pH electrophoresis of the two fractions obtained by affinity chromatography may be useful for investigations on the polymorphism of the casein fractions.