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Journal of Dairy Science Vol. 73 No. 7 1707-1711
© 1990 by American Dairy Science Association ®
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Affinity Chromatography of Ovine Casein

Stefania Dall'olio 1, Roberta Davoli 1, and Vincenzo Russo 1

1 Istituto di Allevamenti Zootecnici, Università di Bologna, Via Fratelli Rosselli, 107-Coviolo, 42100, Reggio Emilia, Italy

Sheep milk casein was separated into two fractions: one containing alphas1-plus ß- and the other alphas2 plus kappa-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.

Key Words: ovine casein • affinity chromatography

Submitted on May 11, 1989
Accepted on January 24, 1990






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