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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1998-2-18
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pubmed:abstractText |
A system was developed to produce recombinant urokinase-type plasminogen activator in Escherichia coli. The urokinase-type plasminogen activator was produced with a 6 x His-tag at the C-terminus which was shown to have the same activity, after refolding, as the wild-type protein. Purification of the recombinant protein to homogeneity (95%) was possible by one-step affinity chromatography under denaturing conditions. As a result, proteolysis by bacterial proteases during purification was avoided. A higher refolding efficiency (40%) and a higher total recovery yield (25%) of the recombinant protein were obtained by this method.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
|
pubmed:issn |
1046-5928
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
279-83
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9425632-Chromatography, Affinity,
pubmed-meshheading:9425632-Cloning, Molecular,
pubmed-meshheading:9425632-Escherichia coli,
pubmed-meshheading:9425632-Humans,
pubmed-meshheading:9425632-Kinetics,
pubmed-meshheading:9425632-Plasmids,
pubmed-meshheading:9425632-Protein Denaturation,
pubmed-meshheading:9425632-Protein Folding,
pubmed-meshheading:9425632-Recombinant Proteins,
pubmed-meshheading:9425632-Restriction Mapping,
pubmed-meshheading:9425632-Sequence Tagged Sites,
pubmed-meshheading:9425632-Urokinase-Type Plasminogen Activator
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pubmed:year |
1997
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pubmed:articleTitle |
An efficient system for production of recombinant urokinase-type plasminogen activator.
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pubmed:affiliation |
Vascular Research Laboratory, Beth Israel-Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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