Interaction between tryptophan residues and hydrophobically modified dextran: Effect on partitioning of peptides and proteins in aqueous two-phase systems
β Scribed by Min Lu; Folke Tjerneld
- Book ID
- 108340925
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 566 KB
- Volume
- 766
- Category
- Article
- ISSN
- 1873-3778
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π SIMILAR VOLUMES
The e β ect of anionic (sodium butylbenzene sulfonate, sodium butylmonoglycol sulfate), cationic (tetrabutyl ammonium bromide), nonionic(Tween 20) and amphoteric (proline) surface active additives on the partitioning of proteins and enzymes, such as BSA, lysozyme, glucose oxidase and b-lactoglobulin,
Two different series of hydrophobically modified proteins were partitioned in a number of aqueous two-phase systems (ATPS) to investigate the effect of hydrophobicity as a single property on partitioning. The modified proteins were derived from P-lactoglobulin and bovine serum albumin (BSA). Measure
## Abstract Correlations to describe the effect of surface hydrophobicity and charge of proteins with their partition coefficient in aqueous twoβphase systems were investigated. Polyethylene glycol (PEG) 4000/phosphate, sulfate, citrate, and dextran systems in the presence of low (0.6% w/w) and hig