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Abstract
Whole casein, αs-casein and k-casein were dephosphorylated with a phosphoprotein phosphatase prepared from beef spleen and their calcium-binding capacities were compared with those of respective native caseins by a ultracentrifugal method.
The bindings of the calcium to 94% dephosphorylated whole casein and to 97 % dephosphorylated αs-casein at neutral pH were approximately one third of those to respective native caseins. The decrease of calcium-binding capacity of k-casein due to dephosphorylation was also significant.
The effect of pH on the state and the calcium-binding capacity of dephosphorylated caseins was also examined and the role of organic phosphate groups of casein as calcium-binding sites was discussed.