Abstract
Buffalo milk casein was separated in main three components, αs-, β- and κ-caseins by acrylamide gel electrophoresis in the presence of 2-mercaptoethanol. Buffalo αs-casein had a slightly slower mobility than bovine αs-casein and revealed three or four accompanying bands. Buffalo and bovine β-caseins have the same mobility. Buffalo κ-casein revealed two bands which have been named earlier, κ-casein A and B, the B-band being more prominent. Buffalo αs-, β- and κ-caseins were isolated by DEAE cellulose column chromatography and by gel electrophoresis to determine their homogeneity and their amino acid composition. Buffalo αs-casein fraction obtained by DEAE cellulose column chromatography revealed three bands on gel electrophoresis and κ-casein fraction revealed two bands. Buffalo β-casein fraction was homogeneous. The amino acid composition of buffalo casein resembled that of bovine casein.
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