The phase behavior of two aqueous binary protein mixtures, lysozyme-chymotrypsin and lysozymeovalbumin, was determined in ammonium sulfate solutions. Protein concentrations were determined in both phases as a function of pH and ionic strength. For lysozyme-chymotrypsin mixtures, the observed phase b
Molecular thermodynamics for fluid-phase equilibria in aqueous two-protein systems
β Scribed by Nicolas von Solms; Camille O. Anderson; Harvey W. Blanch; John M. Prausnitz
- Publisher
- American Institute of Chemical Engineers
- Year
- 2002
- Tongue
- English
- Weight
- 230 KB
- Volume
- 48
- Category
- Article
- ISSN
- 0001-1541
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
A lattice model is presented to compute salt-induced liquid-liquid phase separation in aqueous polymer solutions. The Gibbs energy of mixing contains an electrostatic contribution given by Pitzer's extension of the Debye-Hu Β¨ckel function, and the extended Flory-Huggins theory that uses empirical fu
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
Genetic engineering has been used for the fusion of peptides, with different length and composition, on a protein to study the effect on partitioning in aqueous two-phase systems containing thermoseparating polymers. Peptides containing 2-6 tryptophan residues or tryptophan plus 1-3 lysine or aspart
In this study we show that proteins can be partitioned and separated in a novel aqueous two-phase system composed of only one polymer in water solution. This system represents an attractive alternative to traditional two-phase systems which uses either two polymers (e.g., PEG/dextran) or one polymer