Linked Life Data

8670254

Source:http://linkedlifedata.com/resource/pubmed/id/8670254

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-8-6
pubmed:abstractText
A 65-kDa molecular mass of thiol-specific antioxidant protein was purified from human plasma and identified as human serum albumin (HSA) by the analysis of amino-terminal amino acid sequence. This protein exhibited the preventive effects against the inactivation of glutamine synthetase activity and the peroxidation of lipid by a metal-catalyzed oxidation system. These antioxidant activities were supported by a thiol-reducing equivalent such as DTT and reduced glutathione. The thiol-specific antioxidant activity of HSA was greatly activated by halide ion, especially by chloride ion. HSA showed a significant capability to destroy H2O2 in the presence of reduced glutathione, resulting in the production of oxidized glutathione. Both the preventive activity against the glutamine synthetase inactivation and the peroxidase activity were completely abolished by the reactions of HSA with N-ethylmaleimide and iodoacetate, chemical modification agents for sulfhydryl of protein, only in the presence of thiol-reducing equivalent such as DTT. These results suggest that serum albumin acts as a major and predominate antioxidant exerting a glutathione-linked thiol peroxidase activity which removes reactive oxygen species such as H2O2 within blood plasma.
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
15
pubmed:volume
222
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
619-25
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Glutathione-linked thiol peroxidase activity of human serum albumin: a possible antioxidant role of serum albumin in blood plasma.
pubmed:affiliation
Department of Biochemistry, Pai-Chai University, Taejon, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't