Linked Life Data

11165879

Source:http://linkedlifedata.com/resource/pubmed/id/11165879

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-2-22
pubmed:abstractText
Human Serum Albumin (HSA) exerted a significant lipid peroxidase activity with the use of a thiol-reducing equivalent such as dithiothreitol (DTT). Carboxyl group-modified HSA (CM-HSA) showed a 10-fold stronger lipid peroxidase activity (1.6 nmol/min/mg) than that of HSA (0.17 nmol/min/mg). Instead of DTT, thioredoxin (Trx) also supported reducing equivalent to the reduction of lipid hydroperoxide by CM-HSA. Contrast to CM-HSA, HSA did not reduce lipid peroxide with the use of Trx. In the presence of palmitoyl coenzyme A (palmitoyl-CoA) however, HSA used Trx as an electron donor to the reduction of lipid hydroperoxide. The Trx-linked peroxidase activity of HSA sharply increased with elongation in the carbon chain of the acyl moiety of acyl-CoA, showing an optimum activity in the presence of palmitoyl-CoA. Fluorescence study indicates the conformational changes of HSA induced by palmitoyl-CoA. Together, these data suggest that palmitoyl-CoA-bound HSA has a capability to remove lipid peroxide with the use of electrons given by Trx system.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0891-5849
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
327-33
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Thioredoxin-linked lipid hydroperoxide peroxidase activity of human serum albumin in the presence of palmitoyl coenzyme A.
pubmed:affiliation
Department of Biochemistry, Paichai University, 439-6 Doma-2 Dong Seo-Gu Taejon 302-735, Republic of Korea.
pubmed:publicationType
Journal Article