Study of the dissociation of high-molecular-weight aggregates of preparations of αs1-, β-, κ-, and para-κ-casein by the detergent, sodium dodecyl sulphate (SDS), showed that there are differences in the aggregation properties of the individual caseins. Binding of detergent led first to the dissociation of casein aggregates and then to further interaction with the casein molecules. The amounts of detergent required to give the minimum sized protein-detergent aggregate when expressed as mg/mg casein were similar for κ-, para-κ- and αs1-casein but much less for β-casein. However, expressed as mole/mole the requirement for κ- and αs1-casein was similar but was twice that found for para-κ- and β-casein. The maximum amount of SDS bound was about twice that required for complete dissociation of the aggregates for κ-, para-κ- and αs1-casein but was 13 times greater for β-casein.

Complete dissociation of κ-casein aggregates by SDS alone was not possible due to the presence of aggregates formed by disulphide linkages. These aggregates, which consisted of 3±1 protein molecules, accounted for about one-third of the κ-casein in the preparations examined.