Light-scattering study of effect of electrolytes on α- and β-casein solutions

Solutions of α- and β-casein are aggregated by electrolytes. This contrasts with the behavior of native ovalbumin, serum albumin, and lactoglobulin, but resembles that of the denatured forms of these proteins (the latter two after addition of ethanol). It is concluded that the caseins have the properties of denatured proteins. Determination of their molecular weights is complicated by the aggregation effect, and values in which confidence can be felt probably do not now exist.