Linked Life Data

8554614

Source:http://linkedlifedata.com/resource/pubmed/id/8554614

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-2-22
pubmed:databankReference
pubmed:abstractText
A thiol-dependent antioxidant protein (HRPRP) was previously reported as a predominant antioxidant protein in human red blood cell (RBC). The analysis of amino acid sequence of HRPRP with those of human PRP-like gene products indicates that HRPRP is identical to brain PRP (HPRP). This protein act as a peroxidase linked to thioredoxin (Trx)/thioredoxin reductase (TR). Until now, there was no evidence for Trx/TR system in RBC. The existence of the Trx/TR system in RBC was immunologically determined. A 58-kDa protein showing TR activity was partially purified from human RBC and characterized. Our results reveal that HRPRP act as a new type of peroxidase supported by Trx/TR system in human RBC.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
217
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
900-7
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Thioredoxin-linked peroxidase from human red blood cell: evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell.
pubmed:affiliation
Department of Biochemistry, Pai-Chai University, Taejon, Republic of Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't