The hydrophilic colloid, carrageenan, stabilizes αs-casein against precipitation by calcium ions by an interaction between αs-casein and a component which may be present in both κ- and λ-carrageenan. This component occurs predominantly in the κ-fraction. The resulting complex resembles the alpha-casein complex, but it is not acted upon by rennin. The κ-carrageenan fraction imparted stability when mixed with αs-casein in the weight ratio of 1:5, whereas the λ-carrageenan fraction was fully effective only at a ratio above 2:5. The heat stability of the calcium/carrageenan/αs-casein complex was greater than the corresponding calcium/κ-casein/αs-casein complex. No significant stabilization of αs-casein was produced by chondroitin sulphate, heparin, alginate, carboxymethylcellulose, guar gum, or locust bean gum. © 1968, American Dairy Science Association. All rights reserved.