Linked Life Data

9756741

Source:http://linkedlifedata.com/resource/pubmed/id/9756741

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1998-11-24
pubmed:abstractText
Escherichia coli has been widely used in the production of recombinant proteins. One of the drawbacks inherent in this method is that the proteins produced in the cells often form inactive inclusion bodies. Usually, the inclusion bodies can be separated from other cell components, solubilized by denaturants such as guanidine hydrochloride or urea, and then renatured through a refolding process such as dilution or dialysis. However, it has been shown that biologically active recombinant human neurotrophin-3 cannot be obtained at high yield by this procedure due to aggregation and precipitation of the protein. We applied the refolding process using the aggregation suppressor L-arginine in the renaturation of neurotrophin-3, and obtained biologically active neurotrophin-3 at high yield from the inclusion bodies. Consequently, about 10 mg of purified neurotrophin-3 was prepared from 1 litre of culture broth.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0885-4513
pubmed:author
pubmed:issnType
Print
pubmed:volume
28 ( Pt 2)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
119-24
pubmed:dateRevised
2007-3-21
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Renaturation of recombinant human neurotrophin-3 from inclusion bodies using a suppressor agent of aggregation.
pubmed:affiliation
Biotechnology Laboratories, Pharmaceutical Research Division, Takeda Chemical Industries Ltd, Jusohonmachi 2-17-85, Yodogawa-ku, Osaka 532, Japan.
pubmed:publicationType
Journal Article