Details are given of the method used in this laboratory for the preparation of k-casein. The recovery is about 25% and the material has a purity, estimated from electrophoretic patterns, of about 90% with β-casein as the main contaminant. Higher temperatures and lower ion concentration caused precipitation of k-casein in the presence of calcium ions, 0·1m-acetate buffer at pH 6·5 being sufficient to stabilize a 0·5% solution in the presence of 0·01–0·2m-CaCl2 at 20 and 30°C but not at all calcium concentrations at 40°C. It was also found that solutions of para-k-casein did not aggregate in the presence of concentrations of electrolytes above about 0·25m.

The rate of release of non-protein nitrogen and decline in viscosity during the enzymic stage of gel formation in solutions of k-casein and rennin had similar apparent first order constants (0·087 ± 0·03 min—1 and 0·086 ± 0·021 min—1, respectively, at 25°C). A gel could be formed by rennin action in a solution containing as little as 6·25mg of the protein per litre. In the non-enzymic stage of gelling of k-casein solutions the calculated activation energy over the range of 20–40°C was much lower than that obtained from the non-enzymic stage of milk coagulation.