Physicochemical properties of human/c-casein were studied by ultracentrifugal analysis and circular dichroism (CD) measurement. The result of sedimentation velocity analysis in 50mM imidazole-HCl buffer at pH 7.0 showed that human K-casein was present in a monomerie form with S020, w of 2-7S. Tne molecular weight of this protein was estimated to be 38, 000 by a short column method. The molecular shape was considered to be a flat ellipsoid with the shape factor of 16.74 and with the frictional coefficient of 2.17. From the result of CD measurement, human K-casein was computed to have 2% α-helix, 43% β-sheet and 26% β-turn structures. Interaction of human kcasein with human β-casein was observed by sedimentation velocity analysis and discpolyacrylamide gel electrophoresis, but no association occurred between human jc-casein and human lactoferrin under the conditions we studied.
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Azuma et al. (1984) studied this question.