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Some properties of α s - κ -casein micelles were studied with relation to the importance of protein-bound phosphate groups. Partial dephosphorylation of α s -casein by wheat germ acid phosphate decreased its incorporation into micelles. The micelles formed with dephosphorylated α s -casein were much smaller by electron microscopy than those formed with untreated α s -casein. Protein phosphate groups of α s -casein previously combined in a micelle were hydrolyzed by the acid phosphatase. Hydrolysis of the protein phosphate groups ultimately disrupted the micelle, which was pH dependent. α s - κ -Casein micelles had porous or open structures through which macromolecules, such as acid phosphatase, gained access.