Abstract
Summary Turbidity measurements at zero and 36C showed interactions between isolated casein components in the presence of 0.008 m calcium. Stable casein dispersions were obtained with final concentrations of 0.1 to 1.0 mg/ml, depending upon the component studied. Strong interactions were established for κ -casein with either α s -casein or β -casein. A possible explanation is offered for the fact that the sum of β + κ -caseins can be measured in whole casein by a similar method, although purified components when added to whole casein may cause a decrease in the temperature-sensitive increment. The method can be used to estimate the purity of isolated casein fractions, because of marked changes in turbidity produced by trace amounts of other casein fractions in the purified fraction.
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