| pubmed-article:2894309 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2894309 | lifeskim:mentions | umls-concept:C0042071 | lld:lifeskim |
| pubmed-article:2894309 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:2894309 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:2894309 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:2894309 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2894309 | pubmed:dateCreated | 1988-4-19 | lld:pubmed |
| pubmed-article:2894309 | pubmed:abstractText | Recombinant single-chain urokinase-type plasminogen activator (rscu-PA), in which the plasmin-sensitive peptide bond Lys158-Ile159 is destroyed by site-specific mutagenesis of Lys158 to Glu (rscu-PA-Glu158), is quantitatively converted to two-chain urokinase-type plasminogen activator (rtcu-PA-Glu158) by treatment with endoproteinase Glu-C (Staphylococcus aureus V8 proteinase). The catalytic efficiency (k2/Km) of rscu-PA-Glu158 for the activation of plasminogen is 20 times lower (0.0001 microM-1 s-1) than that of rscu-PA (0.002 microM-1 s-1). In contrast, rtcu-PA-Glu158 has very similar properties to rtcu-PA obtained by digestion of rscu-PA with plasmin, including binding to benzamidine-Sepharose, catalytic efficiency for the activation of plasminogen (0.035 microM-1 s-1 versus 0.046 microM-1 s-1) and fibrinolytic activity in an in vitro plasma clot lysis system. It is concluded that the amino acid in position 158 is a main determinant of the functional properties of single-chain urokinase-type plasminogen activator but not of the two-chain form. | lld:pubmed |
| pubmed-article:2894309 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2894309 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2894309 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2894309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2894309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2894309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2894309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2894309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2894309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2894309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2894309 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2894309 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:2894309 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:2894309 | pubmed:author | pubmed-author:CollenDD | lld:pubmed |
| pubmed-article:2894309 | pubmed:author | pubmed-author:LijnenH RHR | lld:pubmed |
| pubmed-article:2894309 | pubmed:author | pubmed-author:NellesLL | lld:pubmed |
| pubmed-article:2894309 | pubmed:author | pubmed-author:HolmesW EWE | lld:pubmed |
| pubmed-article:2894309 | pubmed:author | pubmed-author:Van HoefBB | lld:pubmed |
| pubmed-article:2894309 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2894309 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2894309 | pubmed:volume | 172 | lld:pubmed |
| pubmed-article:2894309 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2894309 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2894309 | pubmed:pagination | 185-8 | lld:pubmed |
| pubmed-article:2894309 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:2894309 | pubmed:meshHeading | pubmed-meshheading:2894309-... | lld:pubmed |
| pubmed-article:2894309 | pubmed:meshHeading | pubmed-meshheading:2894309-... | lld:pubmed |
| pubmed-article:2894309 | pubmed:meshHeading | pubmed-meshheading:2894309-... | lld:pubmed |
| pubmed-article:2894309 | pubmed:meshHeading | pubmed-meshheading:2894309-... | lld:pubmed |
| pubmed-article:2894309 | pubmed:meshHeading | pubmed-meshheading:2894309-... | lld:pubmed |
| pubmed-article:2894309 | pubmed:meshHeading | pubmed-meshheading:2894309-... | lld:pubmed |
| pubmed-article:2894309 | pubmed:meshHeading | pubmed-meshheading:2894309-... | lld:pubmed |
| pubmed-article:2894309 | pubmed:meshHeading | pubmed-meshheading:2894309-... | lld:pubmed |
| pubmed-article:2894309 | pubmed:meshHeading | pubmed-meshheading:2894309-... | lld:pubmed |
| pubmed-article:2894309 | pubmed:meshHeading | pubmed-meshheading:2894309-... | lld:pubmed |
| pubmed-article:2894309 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2894309 | pubmed:articleTitle | Enzymatic properties of single-chain and two-chain forms of a Lys158----Glu158 mutant of urokinase-type plasminogen activator. | lld:pubmed |
| pubmed-article:2894309 | pubmed:affiliation | Center for Thrombosis and Vascular Research, University of Leuven, Belgium. | lld:pubmed |
| pubmed-article:2894309 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2894309 | lld:pubmed |
