Linked Life Data

9660200

Source:http://linkedlifedata.com/resource/pubmed/id/9660200

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-7-21
pubmed:databankReference
pubmed:abstractText
A 58-kDa protein (ER58) was purified from monkey liver to apparent homogeneity. It accounts for more than 3% of microsomal proteins and is highly conserved among several mammalian species. The amino acid compositions of the N-terminal part and that of two internal peptide fragments present strong similarities with the sequence ascribed to phospholipase C-alpha. Numerous proteins exhibiting a high similarity with this sequence have been isolated by other investigators. Their biological function is controversial. Our purified protein is not active as a phosphatidylinositol-specific phospholipase C, protease or carnitine acyl transferase. Although less efficient than authentic protein-disulfide isomerase, ER58 catalyses the glutathione-dependent reduction of insulin and the reorganization of disulfide bonds of randomly oxidized (scrambled) ribonuclease in reducing conditions. In contrast, ER58 is devoid of oxidizing activity on thiol groups of reduced proteins. Many studies suggest that the proteins bearing the phospholipase C-alpha sequence could be considered as protein-disulfide isomerase isozymes. Our results indicate that ER58 is not totally similar to protein-disulfide isomerase in performing thiol :protein-disulfide oxidoreductase reactions and suggest that the two proteins may exert distinct cellular functions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
254
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
420-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Purification of a 58-kDa protein (ER58) from monkey liver microsomes and comparison with protein-disulfide isomerase.
pubmed:affiliation
INSERM, Unité 128, CNRS, Montpellier, France. bonfils@xerxes.crbm.cnrs-mop.fr
pubmed:publicationType
Journal Article, Comparative Study, In Vitro