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
✍ Scribed by Polyakov, V. I. ;Popello, I. A. ;Grinberg, V. Ya. ;Tolstoguzov, V. B.
- Publisher
- John Wiley and Sons
- Year
- 1986
- Tongue
- English
- Weight
- 447 KB
- Volume
- 30
- Category
- Article
- ISSN
- 0027-769X
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✦ Synopsis
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 ovalbuminbovine serum albumin, caseinsoybean globulin fraction, and ovalbuminthermotropic 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 globulln fraction, Water -Ovalbumin -Thermotropic aggregates of ovalbumin. Intermolecular interactions have been shown to play a signilicant role in the thermodynamics of protein compatibility.