Source:http://linkedlifedata.com/resource/pubmed/id/15642462
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2005-1-11
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pubmed:abstractText |
Interleukin-2 (IL-2) can stimulate T cell proliferation and differentiation when binding to its receptor on T cells. It produces a marked effect by enhancing the cytotoxicity of CD8+ T cells and natural killer cells. Granulocyte-macrophage colony stimulating factor (GM-CSF) is associated with many cells proliferation, such as dendritic cells, macrophages. Here, we report the construction, expression and purification of a bifunctional protein, hIL-2/GM-CSF, which may facilitate interaction between T cells and the antigen presentation cells and improve the efficiency of antigen presentation. We found that the use of chemicals and temperature shift is a peculiar system for induction of the Escherichia coli transformed with an IPTG-regulated hIL-2/GM-CSF expression vector in this research. After renaturation, anion exchange chromatography, metal affinity chromatography, and strict endotoxin-free cation exchange chromatography, the fusion protein devoid of endotoxin showed high purity. Cell proliferation experiments proved that this bifunctional protein retains both hIL-2 and GM-CSF biological activities. These results will facilitate the numerous subsequent studies on this bifunctional molecule.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Endotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Granulocyte-Macrophage...,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Isopropyl Thiogalactoside,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1046-5928
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
39
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
131-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15642462-Blotting, Western,
pubmed-meshheading:15642462-Cell Proliferation,
pubmed-meshheading:15642462-Chromatography, Ion Exchange,
pubmed-meshheading:15642462-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:15642462-Endotoxins,
pubmed-meshheading:15642462-Escherichia coli,
pubmed-meshheading:15642462-Genetic Vectors,
pubmed-meshheading:15642462-Granulocyte-Macrophage Colony-Stimulating Factor,
pubmed-meshheading:15642462-Histidine,
pubmed-meshheading:15642462-Inclusion Bodies,
pubmed-meshheading:15642462-Interleukin-2,
pubmed-meshheading:15642462-Isopropyl Thiogalactoside,
pubmed-meshheading:15642462-Limulus Test,
pubmed-meshheading:15642462-Plasmids,
pubmed-meshheading:15642462-Protein Renaturation,
pubmed-meshheading:15642462-Recombinant Fusion Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
Expression, refolding, purification, and bioactivity of recombinant bifunctional protein, hIL-2/GM-CSF.
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pubmed:affiliation |
Institute of Molecular Immunology, Southern Medical University, Guangzhou 510515, People's Republic of China. wqrv@hotmail.com
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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