Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-9-23
pubmed:abstractText
L-arginine ahs received much attention in numerous aspects of the regulation of vascular tone and haemostasis. L-arginine seems to be capable to bind to plasminogen, too. The aim of the present paper is to investigate the action of L-arginine on in vitro plasmin generation and fibrino(geno)lysis by chromogenic, kinetic plasmin generation assay and electrophoretic analysis. The acceleration of tPA-induced plasmin generation in the presence of low concentration of L-arginine, along with augmentation of in vitro fibrinogenolysis have been documented. L-arginine may have a role in the modification of fibrinogenolysis, and this role should be considered if arginine is used as an element of some novel antithrombotic agents.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0049-3848
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
87
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
75-82
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Effect of L-arginine on in vitro plasmin-generation and fibrinogenolysis.
pubmed:affiliation
2nd Department of Medicine and Institute of Clinical Chemistry, University Medical School, Debrecen, Hungary.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't