Format

Send to

Choose Destination
Biochim Biophys Acta. 2013 Dec;1834(12):2859-66. doi: 10.1016/j.bbapap.2013.07.014. Epub 2013 Aug 3.

Effect of salt additives on protein partition in polyethylene glycol-sodium sulfate aqueous two-phase systems.

Author information

1
AnalizaDx Inc., 3615 Superior Ave., Suite 4407B, Cleveland, OH 44114, USA.

Abstract

Partitioning of 15 proteins in polyethylene glycol (PEG)-sodium sulfate aqueous two-phase systems (ATPS) formed by PEG of two different molecular weights, PEG-600 and PEG-8000 in the presence of different buffers at pH7.4 was studied. The effect of two salt additives (NaCl and NaSCN) on the protein partition behavior was examined. The salt effects on protein partitioning were analyzed by using the Collander solvent regression relationship between the proteins partition coefficients in ATPS with and without salt additives. The results obtained show that the concentration of buffer as well as the presence and concentration of salt additives affects the protein partition behavior. Analysis of ATPS in terms of the differences between the relative hydrophobicity and electrostatic properties of the phases does not explain the protein partition behavior. The differences between protein partitioning in PEG-600-salt and PEG-8000-salt ATPS cannot be explained by the protein size or polymer excluded volume effect. It is suggested that the protein-ion and protein-solvent interactions in the phases of ATPS are primarily important for protein partitioning.

KEYWORDS:

Aqueous two-phase system; Partitioning; Protein structure; Solvent interaction analysis; Structural changes

PMID:
23920121
DOI:
10.1016/j.bbapap.2013.07.014
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center