抄録
The interaction of αS1-casein with β-, dephosphorylated β-, γ- and R-caseins was studied. It was proved by the sedimentation velocity experiments that αSl-casein formed a complex with each of these components at 25°C in the presence of 3mM CaCl2.
In the presence of 10mM CaCl2, β- and dephosphorylated β-casein prevented the precipitation of αS1-casein and gave micelle-like turbid solutions. However, γ- and R-caseins, fragments of β-casein, did not stabilize αS1-casein. It was concluded from these results that β-casein interacted with αS1-casein through its hydropholic region corresponding to R-casein and that hydrophilic region of β-casein was responsible for the stabilization of αS1-casein.
