Abstract
Aqueous solutions of β-lactoglobulin (at the isoelectric point pH=5.18) have been studied by membrane osmometry. The osmotic second virial coefficient as well as the monomer–dimer equilibrium of β-lactoglobulin have been found to depend significantly on the salt concentration. At low salt concentration the virial coefficient becomes negative, which could be attributed to dipole–dipole interactions which become important at the isoelectric point of the protein when the salt concentration decreases.

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