Linked Life Data

9195754

Source:http://linkedlifedata.com/resource/pubmed/id/9195754

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-7-29
pubmed:abstractText
Human protein disulfide isomerase with an extra 10 amino acid residues of AEITRIDPAM at the N-terminal was expressed in E. coli as a soluble protein comprising 20% of total cell proteins, and was purified to near homogeneity through one step of DEAE-Sephacel chromatography. The mutant enzyme, which had the same CD spectrum and comparable disulfide isomerase and thiol-protein oxidoreductase activities with that of the wild type human and bovine protein disulfide isomerases, also showed chaperone-like activity in stimulating the refolding of proteins containing no disulfide bond. The overall yield of the active product is about 20 mg 1-1 culture.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0168-1656
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
54
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
105-12
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Mutant human protein disulfide isomerase assists protein folding in a chaperone-like fashion.
pubmed:affiliation
National Laboratory of Biomacromolecules, Academia Sinica, Beijing, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't