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
Effects of chemical modifications in the partition behavior of proteins in aqueous two-phase systems: A case study with RNase A
✍ Scribed by González-Valdez, José; Rito-Palomares, Marco; Benavides, Jorge
- Book ID
- 120344674
- Publisher
- American Institute of Chemical Engineers
- Year
- 2013
- Tongue
- English
- Weight
- 248 KB
- Volume
- 29
- Category
- Article
- ISSN
- 8756-7938
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
The effect of protein concentration in partitioning in PEG/ salt aqueous two-phase systems has been investigated. PEG 4000lphosphate systems in the presence of 0% wlw and 8.8% wlw NaCl have been evaluated using amyloglucosidase, subtilisin, and trypsin inhibitor. Also, a PEG 4000lphosphate system wi
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
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
## Abstract Aqueous two‐phase partitioning is one of the excellent bioseparation systems for proteins and other biomolecules in water‐rich solutions containing polymers or salts. To improve the partition properties of model proteins, chicken egg white (CEW) proteins were chemically modified with po
## Abstract Correlations to describe the effect of surface hydrophobicity and charge of proteins with their partition coefficient in aqueous two‐phase systems were investigated. Polyethylene glycol (PEG) 4000/phosphate, sulfate, citrate, and dextran systems in the presence of low (0.6% w/w) and hig