Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
2009-10-5
pubmed:abstractText
We studied the effect of acrolein, an alpha,beta-unsaturated aldehyde that causes adduct-modification of lysine, cysteine, and histidine residues, on antithrombin, a key anticoagulant serpin. Intrinsic fluorescence, functionality (anti-FXa and anti-IIa activity), heparin affinity and conformational features of plasma and purified antithrombin were evaluated. In vivo experiments were carried out in mice. Intrinsic fluorescence showed a two-step conformational change. Acrolein, even at low dose, impaired the anticoagulant function of purified antithrombin by affecting its heparin affinity. However, higher concentrations of acrolein and long incubations are required to cause mild functional effects on plasma antithrombin and mice.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1873-3468
pubmed:author
pubmed:issnType
Electronic
pubmed:day
6
pubmed:volume
583
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3165-70
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Effects of acrolein, a natural occurring aldehyde, on the anticoagulant serpin antithrombin.
pubmed:affiliation
Centro Regional de Hemodonación, Universidad de Murcia, Ronda de Garay S/N, Murcia 30003, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't