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Effects of ions on partitioning of serum albumin and lysozyme in aqueous two-phase systems containing ethylene oxide/propylene oxide co-polymers

Johansson, Hans-Olof LU ; Lundh, Gabriella; Karlström, Gunnar LU and Tjerneld, Folke LU (1996) In Biochimica et Biophysica Acta. General Subjects 1290(3). p.289-298
Abstract
Aqueous two-phase systems composed of ethylene oxide/propylene oxide random co-polymers, EO30/PO70 or Ucon (EO50/PO50), in the top phase and dextran T500 in the bottom phase, have been studied. The cloud point diagram for EO30/PO70 in water solution was determined. EO30/PO70 has a cloud point of 32oC at a concentration of 10% (w/w). The phase diagram for the system EO30/PO70-dextran T500-water was determined. Salt effects have been studied on the partitioning of two model proteins, bovine serum albumin and hen egg white lysozyme, in EO30/PO70-dextran and Ucon-dextran systems. Ions with different hydrophobicity, i.e., with different position in the Hofmeister or lyotropic series, were investigated with reference to their effect on protein... (More)
Aqueous two-phase systems composed of ethylene oxide/propylene oxide random co-polymers, EO30/PO70 or Ucon (EO50/PO50), in the top phase and dextran T500 in the bottom phase, have been studied. The cloud point diagram for EO30/PO70 in water solution was determined. EO30/PO70 has a cloud point of 32oC at a concentration of 10% (w/w). The phase diagram for the system EO30/PO70-dextran T500-water was determined. Salt effects have been studied on the partitioning of two model proteins, bovine serum albumin and hen egg white lysozyme, in EO30/PO70-dextran and Ucon-dextran systems. Ions with different hydrophobicity, i.e., with different position in the Hofmeister or lyotropic series, were investigated with reference to their effect on protein partition. The counterion hydrophobicity was shown to have a strong influence on the partitioning of BSA and lysozyme. Most extreme partitioning was obtained with hydrophobic (chaotropic) ions like ClO-4 and I-. A comparison of protein partitioning between PEG-dextran and EO30/PO70-dextran has been done. A more extreme protein partitioning was obtained in the EO30/PO70-dextran containing system. Temperature-induced phase separation was studied with EO30/PO70 at 45oC. Both BSA and lysozyme were completely partitioned to the water phase formed above the cloud point of EO30/PO70. Model calculations, based on Flory-Huggins theory of polymer solutions, have been done which could reproduce the salt effect on the protein partitioning in aqueous-two phase system. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Polymer, Phase separation, Partitioning of protein, Aqueous two-phase system, Temperature-induced phase separation
in
Biochimica et Biophysica Acta. General Subjects
volume
1290
issue
3
pages
289 - 298
publisher
Elsevier
external identifiers
  • scopus:0030582204
ISSN
0304-4165
DOI
10.1016/0304-4165(96)00031-1
language
English
LU publication?
yes
id
c143e026-d2c8-4761-919f-2f36fbdf5c03 (old id 126281)
date added to LUP
2007-07-05 16:08:52
date last changed
2017-08-27 05:34:08
@article{c143e026-d2c8-4761-919f-2f36fbdf5c03,
  abstract     = {Aqueous two-phase systems composed of ethylene oxide/propylene oxide random co-polymers, EO30/PO70 or Ucon (EO50/PO50), in the top phase and dextran T500 in the bottom phase, have been studied. The cloud point diagram for EO30/PO70 in water solution was determined. EO30/PO70 has a cloud point of 32oC at a concentration of 10% (w/w). The phase diagram for the system EO30/PO70-dextran T500-water was determined. Salt effects have been studied on the partitioning of two model proteins, bovine serum albumin and hen egg white lysozyme, in EO30/PO70-dextran and Ucon-dextran systems. Ions with different hydrophobicity, i.e., with different position in the Hofmeister or lyotropic series, were investigated with reference to their effect on protein partition. The counterion hydrophobicity was shown to have a strong influence on the partitioning of BSA and lysozyme. Most extreme partitioning was obtained with hydrophobic (chaotropic) ions like ClO-4 and I-. A comparison of protein partitioning between PEG-dextran and EO30/PO70-dextran has been done. A more extreme protein partitioning was obtained in the EO30/PO70-dextran containing system. Temperature-induced phase separation was studied with EO30/PO70 at 45oC. Both BSA and lysozyme were completely partitioned to the water phase formed above the cloud point of EO30/PO70. Model calculations, based on Flory-Huggins theory of polymer solutions, have been done which could reproduce the salt effect on the protein partitioning in aqueous-two phase system.},
  author       = {Johansson, Hans-Olof and Lundh, Gabriella and Karlström, Gunnar and Tjerneld, Folke},
  issn         = {0304-4165},
  keyword      = {Polymer,Phase separation,Partitioning of protein,Aqueous two-phase system,Temperature-induced phase separation},
  language     = {eng},
  number       = {3},
  pages        = {289--298},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta. General Subjects},
  title        = {Effects of ions on partitioning of serum albumin and lysozyme in aqueous two-phase systems containing ethylene oxide/propylene oxide co-polymers},
  url          = {http://dx.doi.org/10.1016/0304-4165(96)00031-1},
  volume       = {1290},
  year         = {1996},
}