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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1992-12-4
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pubmed:abstractText |
Glu-plasminogen, kringle 1-5, kringle 1-3, and miniplasminogen exhibited strong binding to human umbilical vein endothelial cells (HUVEC). On the other hand, no significant binding was obtained with microplasminogen and kringle 4. Kringle 1-5 and miniplasminogen, which both contained kringle 5, specifically inhibited the binding of plasminogen to HUVEC while kringle 1-3 did not. The results implied plasminogen molecule contained at least two binding sites, with which it interacted HUVEC. The stronger binding site was located in kringle 5 and the weaker one was in kringle 1-3. Kringle 4 and the active site domain exhibited no significant binding to HUVEC. The interaction of plasminogen with HUVEC is mainly through binding site on kringle 5.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
|
pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
30
|
pubmed:volume |
188
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
703-11
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1445315-Amino Acid Sequence,
pubmed-meshheading:1445315-Binding Sites,
pubmed-meshheading:1445315-Cells, Cultured,
pubmed-meshheading:1445315-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1445315-Endothelium, Vascular,
pubmed-meshheading:1445315-Humans,
pubmed-meshheading:1445315-Iodine Radioisotopes,
pubmed-meshheading:1445315-Kinetics,
pubmed-meshheading:1445315-Molecular Weight,
pubmed-meshheading:1445315-Peptide Fragments,
pubmed-meshheading:1445315-Plasminogen,
pubmed-meshheading:1445315-Protein Conformation,
pubmed-meshheading:1445315-Umbilical Veins
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pubmed:year |
1992
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pubmed:articleTitle |
The binding of plasminogen fragments to cultured human umbilical vein endothelial cells.
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pubmed:affiliation |
Department of Biochemistry, Medical College, National Cheng Kung University, Tainan, Taiwan, Republic of China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|