Effect of salt additives on protein partition in polyethylene glycol-sodium sulfate aqueous two-phase systems
authors Ferreira, L; Madeira, PP; Mikheeva, L; Uversky, VN; Zaslavsky, B
nationality International
journal BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
author keywords Partitioning; Protein structure; Aqueous two-phase system; Structural changes; Solvent interaction analysis
keywords COEFFICIENTS; PLATFORM; BUFFER
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 pH 7.4 was studied. The effect of two salt additives (NaCI 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. (C) 2013 Elsevier B.V. All rights reserved.
publisher ELSEVIER SCIENCE BV
issn 1570-9639
year published 2013
volume 1834
issue 12
beginning page 2859
ending page 2866
digital object identifier (doi) 10.1016/j.bbapap.2013.07.014
web of science category Biochemistry & Molecular Biology; Biophysics
subject category Biochemistry & Molecular Biology; Biophysics
unique article identifier WOS:000329418300043
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journal impact factor 2.371
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