Polyakov V I, Popello I A, Tolstoguzov V B
Nahrung. 1986;30(1):81-8. doi: 10.1002/food.19860300122.
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.
采用流动微量量热法测定了卵清蛋白、牛血清白蛋白、酪蛋白、大豆球蛋白级分、卵清蛋白的热致聚集体、卵清蛋白 - 牛血清白蛋白混合物、酪蛋白 - 大豆球蛋白级分以及卵清蛋白 - 卵清蛋白热致聚集体在水中的稀释焓。将获得的量热数据与水 - 卵清蛋白 - 牛血清白蛋白体系、水 - 酪蛋白 - 大豆球蛋白级分体系、水 - 卵清蛋白 - 卵清蛋白热致聚集体体系的相平衡数据进行了比较。结果表明，分子间相互作用在蛋白质相容性的热力学中起着重要作用。
