Isolation, Purification, and Analysis of Two κ-Casein-like Fractions from Sheep Casein

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Abstract
Two X-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 3 major electro-phoretic components. After rennin digestion, they gave a high proportion of nonprotein nitrogen. Characteristic sheep X-caseino-glycopeptides were isolated and analyzed. In spite of some specific differences concerning mainly the electrophoretic mobility, the sugar composition and the rate of hydrolysis by rennin, the cow and sheep X-caseins are very similar and are digested in a similar manner by rennin.