pubmed-article:7544349 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7544349 | lifeskim:mentions | umls-concept:C0042071 | lld:lifeskim |
pubmed-article:7544349 | lifeskim:mentions | umls-concept:C0030190 | lld:lifeskim |
pubmed-article:7544349 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:7544349 | pubmed:issue | 34 | lld:pubmed |
pubmed-article:7544349 | pubmed:dateCreated | 1995-9-28 | lld:pubmed |
pubmed-article:7544349 | pubmed:abstractText | Urokinase (u-PA) is synthesized and secreted as a single-chain polypeptide (single-chain u-PA, scu-PA), which has such little enzymatic activity in solution that it has been considered essentially enzymatically inert. We found that plasminogen activator inhibitor type 1 (PAI-1), the major PAI in plasma, demonstrated concentration-dependent inhibition of this solution-phase scu-PA enzymatic activity. 125I-scu-PA formed complexes with PAI-1 in a concentration- and time-dependent manner, as detected by SDS-polyacrylamide gel electrophoresis under reducing conditions. Among a given population of scu-PA molecules, all measurable enzymatic activity was inhibited by a 10-fold molar excess of PAI-1. However, at this stoichiometry, only a minority of 125I-scu-PA molecules formed SDS-stable complexes with PAI-1 (i.e. complexes that formed a covalent bond upon denaturation), even though the uncomplexed PAI-1 molecules remained competent to inhibit u-PA enzymatic activity. Neither the extent nor the time course of complex formation was altered by using PAI-1 that had been pre-incubated with native human vitronectin, compared with native PAI-1 alone. 125I-scu-PA.PAI-1 complexes that would form a covalent bond if denatured were reversible and existed in equilibrium with either non-complexed or loosely complexed reactants. These data suggest that scu-PA has more enzyme-like properties than previously appreciated and raises the possibility that it resembles single-chain tissue type-plasminogen activator in lacking a complete zymogen conformation. | lld:pubmed |
pubmed-article:7544349 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7544349 | pubmed:language | eng | lld:pubmed |
pubmed-article:7544349 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7544349 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7544349 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7544349 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7544349 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7544349 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7544349 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7544349 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7544349 | pubmed:month | Aug | lld:pubmed |
pubmed-article:7544349 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:7544349 | pubmed:author | pubmed-author:SchwartzB SBS | lld:pubmed |
pubmed-article:7544349 | pubmed:author | pubmed-author:ManchandaNN | lld:pubmed |
pubmed-article:7544349 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7544349 | pubmed:day | 25 | lld:pubmed |
pubmed-article:7544349 | pubmed:volume | 270 | lld:pubmed |
pubmed-article:7544349 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7544349 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7544349 | pubmed:pagination | 20032-5 | lld:pubmed |
pubmed-article:7544349 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
pubmed-article:7544349 | pubmed:meshHeading | pubmed-meshheading:7544349-... | lld:pubmed |
pubmed-article:7544349 | pubmed:meshHeading | pubmed-meshheading:7544349-... | lld:pubmed |
pubmed-article:7544349 | pubmed:meshHeading | pubmed-meshheading:7544349-... | lld:pubmed |
pubmed-article:7544349 | pubmed:meshHeading | pubmed-meshheading:7544349-... | lld:pubmed |
pubmed-article:7544349 | pubmed:meshHeading | pubmed-meshheading:7544349-... | lld:pubmed |
pubmed-article:7544349 | pubmed:meshHeading | pubmed-meshheading:7544349-... | lld:pubmed |
pubmed-article:7544349 | pubmed:meshHeading | pubmed-meshheading:7544349-... | lld:pubmed |
pubmed-article:7544349 | pubmed:meshHeading | pubmed-meshheading:7544349-... | lld:pubmed |
pubmed-article:7544349 | pubmed:meshHeading | pubmed-meshheading:7544349-... | lld:pubmed |
pubmed-article:7544349 | pubmed:meshHeading | pubmed-meshheading:7544349-... | lld:pubmed |
pubmed-article:7544349 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7544349 | pubmed:articleTitle | Interaction of single-chain urokinase and plasminogen activator inhibitor type 1. | lld:pubmed |
pubmed-article:7544349 | pubmed:affiliation | Department of Medicine, University of Wisconsin, Madison, USA. | lld:pubmed |
pubmed-article:7544349 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7544349 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:7544349 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:7544349 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7544349 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7544349 | lld:pubmed |