rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
|
pubmed:dateCreated |
1999-3-29
|
pubmed:abstractText |
An efficient Escherichia coli expression system for the production of a perchloric acid-soluble protein (PSP) has been constructed. Complementary DNA encoding PSP was inserted into an inducible bacterial expression vector pGEX-4T-1. After the plasmid introduced into E. coli was expressed by isopropyl 1-thio-beta-D-galaetopyranoside (IPTG), the recombinant product was purified by glutathione-Sepharose 4B affinity chromatography. The purified product showed the expected NH2-terminal sequence, but the translation inhibitory activity of this product was 10 times lower compared with that of authentic PSP isolated from rat liver.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
1420-682X
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
55
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
131-4
|
pubmed:dateRevised |
2008-11-21
|
pubmed:meshHeading |
|
pubmed:year |
1999
|
pubmed:articleTitle |
Production of functional rat liver PSP protein in Escherichia coli.
|
pubmed:affiliation |
Department of Veterinary Physiology, Faculty of Agriculture, Kagoshima University, Japan. oka@vet.agri.kagoshima-u.ac.jp
|
pubmed:publicationType |
Journal Article
|