Genetically engineered charge modifications to enhance protein separation in aqueous two-phase systems: Electrochemical partitioning
β Scribed by John R. Luther; Charles E. Glatz
- Publisher
- John Wiley and Sons
- Year
- 1994
- Tongue
- English
- Weight
- 762 KB
- Volume
- 44
- Category
- Article
- ISSN
- 0006-3592
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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
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
Relatively conservative modifications of three proteins were carried out to alter their surface properties. The protein properties modified were hydrophobicity and charge. This was done by acylation of amino groups with anhydrides. For the hydrophobic modification experiments, two proteins (p-lactog
A series of charge-modified thaumatins with different values of surface charge were partitioned in aqueous twophase systems (ATPS) to study the effect of surface charge as a single property on partitioning. Electrophoretic mobility of the proteins in titration curves was used as a measure of surface