Linked Life Data

12244482

Source:http://linkedlifedata.com/resource/pubmed/id/12244482

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-9-23
pubmed:abstractText
A homogeneous set of low-molecular weight heparins, chemically modified to yield different degrees of sulfation, were investigated for their ability to interfere with the antithrombin (AT)-factor Xa (FXa) interaction process in the presence or absence of physiological concentrations of calcium ions. The heparin-AT dissociation constants were not appreciably affected by the presence of the metal ion, whereas the catalytic process was strongly dependent on Ca 2+. Our data suggest that AT binding to heparin represents the main factor driving the FXa inhibition process. In addition, the presence of the metal ion is likely to mask favorable AT- heparin ionic contacts occurring with the highly sulfated material. These results help in assessing proper structure-activity relationships for glycosaminoglycans, a multitarget family of biologically active compounds.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0094-6176
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
355-60
pubmed:dateRevised
2006-3-7
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Effects of calcium ions on the interactions between antithrombin and factor Xa mediated by variously sulfated, semisynthetic low-molecular-weight heparins.
pubmed:affiliation
Department of Pharmaceutical Sciences, University of Padova, Italy. Claudia.sissi@unipd.it
pubmed:publicationType
Journal Article