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Abstract
Sheep milk casein was separated into two fractions: one containing αs1-plus β- and the other αs2 plus κ-caseins by affinity 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.
Published Version
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