| pubmed-article:9003434 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9003434 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:9003434 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:9003434 | lifeskim:mentions | umls-concept:C1521970 | lld:lifeskim |
| pubmed-article:9003434 | lifeskim:mentions | umls-concept:C0032140 | lld:lifeskim |
| pubmed-article:9003434 | lifeskim:mentions | umls-concept:C0242210 | lld:lifeskim |
| pubmed-article:9003434 | lifeskim:mentions | umls-concept:C1414402 | lld:lifeskim |
| pubmed-article:9003434 | lifeskim:mentions | umls-concept:C2364020 | lld:lifeskim |
| pubmed-article:9003434 | lifeskim:mentions | umls-concept:C0870432 | lld:lifeskim |
| pubmed-article:9003434 | lifeskim:mentions | umls-concept:C1705417 | lld:lifeskim |
| pubmed-article:9003434 | lifeskim:mentions | umls-concept:C1704222 | lld:lifeskim |
| pubmed-article:9003434 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:9003434 | lifeskim:mentions | umls-concept:C1555465 | lld:lifeskim |
| pubmed-article:9003434 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:9003434 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:9003434 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:9003434 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9003434 | pubmed:dateCreated | 1997-2-21 | lld:pubmed |
| pubmed-article:9003434 | pubmed:abstractText | Plasminogen binds with low affinity in a lysine-dependent manner to many cell types. Previously, a 54 kDa plasminogen receptor found on the surface of U-937 cells was identified as an alpha-enolase-like molecule. The aims of this study were to determine whether recombinant alpha-enolase (r-alpha-enolase), encoded by ENO1, was a plasminogen binding protein and to generate polyclonal antibodies against this antigen. Plasminogen specifically bound r-alpha-enolase with a Kd 1.9 microM and approached saturation at 10 microM. Lysine-dependent plasminogen binding to r-alpha-enolase was demonstrated by a greater than 80% inhibition of binding by the lysine analogues epsilon-amino caproic acid and tranexamic acid, whilst only 14% inhibition occurred with the arginine analogue benzamidine. Removal of the C-terminal lysine residue of r-alpha-enolase with carboxy-peptidase B significantly reduced its plasminogen binding capacity, suggesting that binding required C-terminal lysine residue of r-alpha-enolase. Binding to r-alpha-enolase enhanced the activation rate of plasminogen by urokinase but prevented alpha 2-antiplasmin from binding plasminogen. Taken together, these data suggest that the gene product of human ENO1 encodes an authentic plasminogen binding protein. | lld:pubmed |
| pubmed-article:9003434 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9003434 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9003434 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9003434 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9003434 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9003434 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:9003434 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:9003434 | pubmed:author | pubmed-author:CANGASS | lld:pubmed |
| pubmed-article:9003434 | pubmed:author | pubmed-author:BognackiJJ | lld:pubmed |
| pubmed-article:9003434 | pubmed:author | pubmed-author:RansonMM | lld:pubmed |
| pubmed-article:9003434 | pubmed:author | pubmed-author:AndronicosN... | lld:pubmed |
| pubmed-article:9003434 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9003434 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:9003434 | pubmed:volume | 1337 | lld:pubmed |
| pubmed-article:9003434 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9003434 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9003434 | pubmed:pagination | 27-39 | lld:pubmed |
| pubmed-article:9003434 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:9003434 | pubmed:meshHeading | pubmed-meshheading:9003434-... | lld:pubmed |
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| pubmed-article:9003434 | pubmed:meshHeading | pubmed-meshheading:9003434-... | lld:pubmed |
| pubmed-article:9003434 | pubmed:meshHeading | pubmed-meshheading:9003434-... | lld:pubmed |
| pubmed-article:9003434 | pubmed:meshHeading | pubmed-meshheading:9003434-... | lld:pubmed |
| pubmed-article:9003434 | pubmed:meshHeading | pubmed-meshheading:9003434-... | lld:pubmed |
| pubmed-article:9003434 | pubmed:meshHeading | pubmed-meshheading:9003434-... | lld:pubmed |
| pubmed-article:9003434 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9003434 | pubmed:articleTitle | The human ENO1 gene product (recombinant human alpha-enolase) displays characteristics required for a plasminogen binding protein. | lld:pubmed |
| pubmed-article:9003434 | pubmed:affiliation | Department of Biological Sciences, Institute for Molecular Recognition, University of Wollongong, NSW, Australia. | lld:pubmed |
| pubmed-article:9003434 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9003434 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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