Linked Life Data

7911017

Source:http://linkedlifedata.com/resource/pubmed/id/7911017

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-6-29
pubmed:abstractText
A protector protein from Saccharomyces cerevisiae specifically prevents the inactivation of enzymes caused by a thiol/Fe3+/O2 metal-catalyzed oxidation system but not by an ascorbate/Fe3+/O2 system. Ascorbate/Fe3+/O2-mediated damage of enzymes could be prevented by the protector protein only in the presence of reduced thiol. We demonstrate that two proteins from yeast, thioredoxin plus another protein having properties similar to that expected to thioredoxin reductase, when presented with NADPH and the yeast protector protein prevented inactivation of E. coli glutamine synthetase by the ascorbate/Fe3+/O2 system. This system also removes hydrogen peroxide effectively. We also demonstrate evidence suggesting that the NADPH-dependent thioredoxin system reactivates protector protein by reversible disulfide-dithiols exchange.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
201
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8-15
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Inhibition of metal-catalyzed oxidation systems by a yeast protector protein in the presence of thioredoxin.
pubmed:affiliation
Department of Food and Nutrition, Chonnam National University, Kwangju, Korea.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't