A suspension of casein micelles in a milk-salts solution bound highly cationic polypeptides and charged surfactants extensively, and globular proteins and low molecular weight amines less extensively. All additives were bound equally to native micelles and to a rennet coagulum. The distribution of each additive between the micellar and soluble phases was constant over a wide range of concentration, indicating that the micelle contained a large number of equivalent binding sites. Additives that did not bind Ca2+ caused a decrease in the rennet coagulation time which was related to the charge on the additive and the amount adsorbed. Salmine affected the time course of the viscosity of milk treated with rennet in a similar way to increase in temperature, accelerating the aggregation phase. Extensively-bound additives protected milk against loss of coagulability by rennet on heating, but did not affect the extent of whey protein denaturation. They did not cause aggregation of micelles or produce significant changes in their size distribution, but did cause a decrease in micellar hydration. It was concluded that the additives were bound to the apatite and casein components of the micelle, causing a change in the environment of the κ-casein and para-κ-casein, which affected their properties.