1979 Volume 43 Issue 6 Pages 1301-1308
k-Casein components having various carbohydrate contents were prepared by diethyl-aminoethyl-cellulose chromatography and the interactions of each k-casein component both with αs1, -casein and with β-casein were examined by Sepharose 4B gel chromatography, ultra-centrifugal experiments and viscosity measurements. Each k-casein component could form complex with αs1- and β-casein in the absence and presence of CaCl2. Molecular weight of complexes of unfractionated k-casein both with αs1, -casein and with β-casein were about 70×104 at 37°C in the absence of CaCl2, while those of complexes of each k-casein component with αs1- and β-casein were about 50×104. Stokes radii of complexes increased with increasing calcium ion. While sedimentation coefficient at 37°C of complex with β-casein had almost the same value, those of complexes with αs1-casein decreased with increase of carbohydrate content of k-casein components. Intrinsic viscosity of complex of k-casein component having much carbohydrate was almost the same among tested temperatures. It is suggested that heterogeneity of k-casein is necessary to form large complex and that the carbohydrate moiety of k-casein contributes the stability of casein complex.
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