The interaction of β-lactoglobulin and κ-casein at high temperature was studied polarimetrically. The rate of interaction was related to the genetic variant of β-lactoglobulin present. β-Lactoglobulin B, whose thermodenaturation was faster than that of A variant, interacted more rapidly with κ-casein than did the A variant. Velocity sedimentation studies indicated that characteristics of the complex were determined more by the β-lactoglobulin than by the κ-casein. The presence of κ-casein during the thermodenaturation of β-lactoglobulin appeared to prevent the aggregation of β-lactoglobulin from proceeding to completion, the κ-casein complexing with intermediate species and restricting the aggregation process.