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.
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.
Polyakov
V I
VI
Popello
I A
IA
Grinberg VYa
Tolstoguzov
V B
VB
D000818:Animals; D002151:Calorimetry; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D006863:Hydrogen-Ion Concentration; D010047:Ovalbumin / Q000032:analysis; D011506:Proteins / Q000032:analysis*; D012710:Serum Albumin, Bovine / Q000032:analysis; D013816:Thermodynamics
D011506:Proteins; D012710:Serum Albumin, Bovine; D010047:Ovalbumin