PEG activation and ligand binding for the affinity partitioning of proteins in aqueous two-phase systems
β Scribed by B. A. Andrews; D. M. Head; P. Dunthorne; J. A. Asenjo
- Publisher
- Springer-Verlag
- Year
- 1990
- Tongue
- English
- Weight
- 366 KB
- Volume
- 4
- Category
- Article
- ISSN
- 0951-208X
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β¦ Synopsis
PEG has been activated using epoxy-oxirane, epichlorohydrin and periodate based reactions. The coupling to activated PEG of several protein ligands of different sizes was investigated. Glutathione, trypsin inhibitor, Protein A and anti-BSA have been bound to PEG and used to increase the selectivity of protein separation in aqueous two-phase systems.
π SIMILAR VOLUMES
The electrochemical effect of a charged dextran derivative and the hydrophobic effect of hydrophobic chain PEG derivative on partitioning of six types of proteins in PEGjdextran aqueous two-phase systems were investigated. When 1. 6%(w/u)DEAE-dextran was present in the system ,the partition coeffici
The effect on the partition of erythrocytes in a two phase aqueous polymer system based on dextran T500 and polyethylene glycol (PEG) 8000 of a combination of immunoaffinity ligands, namely, rabbit immunoglobulin G (IgG) and PEG 1900-modified monoclonal IgG, was examined as a potential cell separati