Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-2-18
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1046-5928
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
279-83
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
An efficient system for production of recombinant urokinase-type plasminogen activator.
pubmed:affiliation
Vascular Research Laboratory, Beth Israel-Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't