Electrostatic potentials and protein partitioning in aqueous two-phase systems
β Scribed by C. A. Haynes; J. Carson; H. W. Blanch; J. M. Prausnitz
- Publisher
- American Institute of Chemical Engineers
- Year
- 1991
- Tongue
- English
- Weight
- 828 KB
- Volume
- 37
- Category
- Article
- ISSN
- 0001-1541
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π SIMILAR VOLUMES
Protein partitioning in aqueous two-phase systems based on phase-forming polymers is strongly affected by the net charge of the protein, but a thermodynamic description of the charge effects has been hindered by conflicting results. Many of the difficulties could be because of problems in isolating
During recombinant E. coli fermentation with high-expression levels inclusion bodies are often formed. Aqueous two-phase systems have been successfully used in the presence of urea for the initial recovery step of inclusion bodies from E. coli. Basic studies of the complex interactions are lacking.
Phase diagram data at 4Β°C was determined for the aqueous two-phase systems composed of polyethylene glycol, dextran, and water. The Flory-Huggins theory of polymer thermodynamics was used to correlate partitioning of biomolecules in these aqueous two-phase systems resulting in a simple linear relati
Two-polymer aqueous phase systems are described in which ribosomes selectively partition into one of the phases. One of the phase systems is used to determine rapidly and conveniently binding of thiostrepton and erythromycin to Escherichia co/i ribosomes under equilibrium conditions.