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Isolation, Purification, and Analysis of Two -Casein-like Fractions from Sheep Casein^1,2,

Dairy Department, University of Nancy and Department of Biochemistry, Faculty of Sciences, University of Paris, France

ABSTRACT

Two -fractions were isolated and purified from whole sheep casein. Their amino acid compositions were closely related and their sugar contents very low. Each of these fractions contained three major electrophoretic compounds. After rennin digestion, they gave a high proportion of nonprotein nitrogen. Characteristic sheep -caseino-glycopeptides were isolated and analyzed. In spite of some specific differences concerning mainly the electrophoretic mobility, the sugar composition, and rate of hydrolysis by rennin, the cow and sheep -caseins are very similar and are digested in a similar manner by rennin.

¹ Sixteenth communication on caseins. Fifteenth communication, see Delfour, A., Alais, C, and Jollès, P. (1966). Chimia, 20:148.

² This research was supported in part by grant FG-FE-112 from the United States Department of Agriculture.