| pubmed-article:10578095 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10578095 | lifeskim:mentions | umls-concept:C0043047 | lld:lifeskim |
| pubmed-article:10578095 | lifeskim:mentions | umls-concept:C0032521 | lld:lifeskim |
| pubmed-article:10578095 | lifeskim:mentions | umls-concept:C0597301 | lld:lifeskim |
| pubmed-article:10578095 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:10578095 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:10578095 | lifeskim:mentions | umls-concept:C0599956 | lld:lifeskim |
| pubmed-article:10578095 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10578095 | pubmed:dateCreated | 2000-2-7 | lld:pubmed |
| pubmed-article:10578095 | pubmed:abstractText | In this study we show that proteins can be partitioned and separated in a novel aqueous two-phase system composed of only one polymer in water solution. This system represents an attractive alternative to traditional two-phase systems which uses either two polymers (e.g., PEG/dextran) or one polymer in high-salt concentration (e.g., PEG/salt). The polymer in the new system is a linear random copolymer composed of ethylene oxide and propylene oxide groups which has been hydrophobically modified with myristyl groups (C(14)H(29)) at both ends (HM-EOPO). This polymer thermoseparates in water, with a cloud point at 14 degrees C. The HM-EOPO polymer forms an aqueous two-phase system with a top phase composed of almost 100% water and a bottom phase composed of 5-9% HM-EOPO in water when separated at 17-30 degrees C. The copolymer is self-associating and forms micellar-like structures with a CMC at 12 microM (0.01%). The partitioning behavior of three proteins (lysozyme, bovine serum albumin, and apolipoprotein A-1) in water/HM-EOPO two-phase systems has been studied, as well as the effect of various ions, pH, and temperature on protein partitioning. The amphiphilic protein apolipoprotein A-1 was strongly partitioned to the HM-EOPO-rich phase within a broad-temperature range. The partitioning of hydrophobic proteins can be directed with addition of salt. Below the isoelectric point (pI) BSA was partitioned to the HM-EOPO-rich phase and above the pI to the water phase when NaClO(4)was added to the system. Lysozyme was directed to the HM-EOPO phase with NaClO(4), and to the water phase with Na-phosphate. The possibility to direct protein partitioning between water and copolymer phases shows that this system can be used for protein separations. This was tested on purification of apolipoprotein A-1 from human plasma and Escherichia coli extract. Apolipoprotein A-1 could be recovered in the HM-EOPO-rich phase and the majority of contaminating proteins in the water phase. By adding a new water/buffer phase at higher pH and with 100 mM NaClO(4), and raising the temperature for separation, the apolipoprotein A-1 could be back-extracted from the HM-EOPO phase into the new water phase. This novel system has a strong potential for use in biotechnical extractions as it uses only one polymer and can be operated at moderate temperatures and salt concentrations and furthermore, the copolymer can be recovered. | lld:pubmed |
| pubmed-article:10578095 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10578095 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578095 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10578095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10578095 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10578095 | pubmed:issn | 0006-3592 | lld:pubmed |
| pubmed-article:10578095 | pubmed:author | pubmed-author:PerssonJJ | lld:pubmed |
| pubmed-article:10578095 | pubmed:author | pubmed-author:TjerneldFF | lld:pubmed |
| pubmed-article:10578095 | pubmed:author | pubmed-author:JohanssonH... | lld:pubmed |
| pubmed-article:10578095 | pubmed:copyrightInfo | Copyright 1999 John Wiley & Sons, Inc. | lld:pubmed |
| pubmed-article:10578095 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10578095 | pubmed:volume | 66 | lld:pubmed |
| pubmed-article:10578095 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10578095 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10578095 | pubmed:pagination | 247-57 | lld:pubmed |
| pubmed-article:10578095 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:10578095 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10578095 | pubmed:articleTitle | Thermoseparating water/polymer system: a novel one-polymer aqueous two-phase system for protein purification. | lld:pubmed |
| pubmed-article:10578095 | pubmed:affiliation | Department of Biochemistry, Lund University, P.O.B. 124, S-221 00, Lund, Sweden. | lld:pubmed |
| pubmed-article:10578095 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10578095 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
