pubmed-article:20236092 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20236092 | lifeskim:mentions | umls-concept:C0014833 | lld:lifeskim |
pubmed-article:20236092 | lifeskim:mentions | umls-concept:C0218986 | lld:lifeskim |
pubmed-article:20236092 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
pubmed-article:20236092 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:20236092 | pubmed:dateCreated | 2010-4-15 | lld:pubmed |
pubmed-article:20236092 | pubmed:abstractText | The expression of rhIL-2 (recombinant human interleukin-2) in bacteria results in the formation of insoluble inclusion-body aggregates. These aggregates were first solubilized under denaturing conditions (sodium phosphate buffer solution containing 8 M urea and 10 mM 2-mercaptoethanol) and then purified using IMAC (immobilized metal-ion-affinity chromatography). IMAC was used to capture rhIL-2. The protein was gradually refolded on the column by a gradient elution (8 M to 0 M urea) in the presence of 10% (v/v) glycerol. Glycerol was used to prevent protein aggregation during the refolding step. Using this method, rhIL-2 was collected at 97% purity and its activity was measured by the lymphocyte transformation test. The measured activity was identical with commercial human interleukin-2. | lld:pubmed |
pubmed-article:20236092 | pubmed:language | eng | lld:pubmed |
pubmed-article:20236092 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20236092 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20236092 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20236092 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20236092 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20236092 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20236092 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20236092 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20236092 | pubmed:month | Apr | lld:pubmed |
pubmed-article:20236092 | pubmed:issn | 1470-8744 | lld:pubmed |
pubmed-article:20236092 | pubmed:author | pubmed-author:PourpakZahraZ | lld:pubmed |
pubmed-article:20236092 | pubmed:author | pubmed-author:ShojaosadatiS... | lld:pubmed |
pubmed-article:20236092 | pubmed:author | pubmed-author:Hashemi-Najaf... | lld:pubmed |
pubmed-article:20236092 | pubmed:author | pubmed-author:EsfandiarSama... | lld:pubmed |
pubmed-article:20236092 | pubmed:author | pubmed-author:SarrafzadehSh... | lld:pubmed |
pubmed-article:20236092 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20236092 | pubmed:volume | 55 | lld:pubmed |
pubmed-article:20236092 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20236092 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20236092 | pubmed:pagination | 209-14 | lld:pubmed |
pubmed-article:20236092 | pubmed:dateRevised | 2010-9-1 | lld:pubmed |
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pubmed-article:20236092 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20236092 | pubmed:articleTitle | Purification and refolding of Escherichia coli-expressed recombinant human interleukin-2. | lld:pubmed |
pubmed-article:20236092 | pubmed:affiliation | Biotechnology Group, Chemical Engineering Department, Tarbiat Modares University, P.O. Box 14115-143, Tehran, Iran. | lld:pubmed |
pubmed-article:20236092 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20236092 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |