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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2009-5-4
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pubmed:abstractText |
Escherichia coli has been most widely used for the production of valuable recombinant proteins. However, over-production of heterologous proteins in E. coli frequently leads to their misfolding and aggregation yielding inclusion bodies. Previous attempts to refold the inclusion bodies into bioactive forms usually result in poor recovery and account for the major cost in industrial production of desired proteins from recombinant E. coli. Here, we describe the successful use of the immobilized folding machineries for in vitro refolding with the examples of high yield refolding of a ribonuclease A (RNase A) and cyclohexanone monooxygenase (CHMO).
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-10052357,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-10508629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-11287237,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-11823179,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-11934294,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-11934300,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-12915732,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-1369303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-1369317,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-1369490,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-1429594,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-15464382,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-15529165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-15652195,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-15695804,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-15830945,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-2110823,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-2177829,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-9108018,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-9217264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-9496669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19323835-9707566
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immobilized Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidylprolyl Isomerase,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Disulfide-Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease, Pancreatic,
http://linkedlifedata.com/resource/pubmed/chemical/cyclohexanone oxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/dsbA protein, E coli
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pubmed:status |
MEDLINE
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pubmed:issn |
1472-6750
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:19323835-Circular Dichroism,
pubmed-meshheading:19323835-Cysteine,
pubmed-meshheading:19323835-Escherichia coli,
pubmed-meshheading:19323835-Escherichia coli Proteins,
pubmed-meshheading:19323835-Humans,
pubmed-meshheading:19323835-Immobilized Proteins,
pubmed-meshheading:19323835-Molecular Chaperones,
pubmed-meshheading:19323835-Oxygenases,
pubmed-meshheading:19323835-Peptidylprolyl Isomerase,
pubmed-meshheading:19323835-Plasmids,
pubmed-meshheading:19323835-Proline,
pubmed-meshheading:19323835-Protein Disulfide-Isomerases,
pubmed-meshheading:19323835-Protein Folding,
pubmed-meshheading:19323835-Ribonuclease, Pancreatic,
pubmed-meshheading:19323835-Spectrometry, Mass, Matrix-Assisted Laser...
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pubmed:year |
2009
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pubmed:articleTitle |
Folding machineries displayed on a cation-exchanger for the concerted refolding of cysteine- or proline-rich proteins.
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pubmed:affiliation |
Department of Agricultural Biotechnology, Seoul National University, Seoul 151-921, Korea. dlee@bioeng.ucsd.edu
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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