Linked Life Data

3144771

Source:http://linkedlifedata.com/resource/pubmed/id/3144771

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1989-1-31
pubmed:abstractText
Binding affinity of fibrinolytic factors to insolubilized lysine and fibrin was quantitatively measured by frontal affinity chromatography using lysine-Toyopearl and fibrin-Sepharose column. The highest binding affinity was found with recombinant tissue-type plasminogen activator (t-PA), followed by lysyl-plasminogen and glutamyl-plasminogen (Glu-PLg) with intermediate affinity, but very low affinity by single chain UK-type plasminogen activator, high molecular weight UK and low molecular weight UK. At the coexistence of EACA, fibrin-binding affinity of Glu-PLg was greatly reduced, but those of UK's were substantially unchanged. It was concluded that high fibrin-binding affinity of t-PA and plasminogens were largely related to the lysine-binding affinity of these enzymes, but that of UK's would be related to the other binding affinity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0049-3848
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
81-90
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Quantitative analysis of fibrin-binding affinity of fibrinolytic components by frontal affinity chromatography.
pubmed:affiliation
Department of Medicine, School of Medicine, Teikyo University, Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't