Thermodynamic compatibility of proteins in aqueous media Part 3. Studies on the role of intermolecular interactions in the thermodynamics of compatibility of proteins according to the data of dilution enthalpies

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Abstract
The flow microcalorimetric method was used to determine the enthalpies of diluting solutions of ovalbumin, bovine serum albumin, casein, soybean globulin fraction, thermotropic aggregates of ovalbumin, mixtures of ovalbumin – bovine serum albumin, casein – soybean globulin fraction, and ovalbumin – thermotropic aggregates of ovalbumin in water. The calorimetric data obtained were compared with the data on phase equilibrium in the systems Water – Ovalbumin – Bovine serum albumin, Water – Casein – Soybean globulin fraction, Water – Ovalbumin – Thermotropic aggregates of ovalbumin. Intermolecular interactions have been shown to play a significant role in the thermodynamics of protein compatibility.