| pubmed-article:1911857 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1911857 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:1911857 | lifeskim:mentions | umls-concept:C0030190 | lld:lifeskim |
| pubmed-article:1911857 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:1911857 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:1911857 | lifeskim:mentions | umls-concept:C0037506 | lld:lifeskim |
| pubmed-article:1911857 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:1911857 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:1911857 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:1911857 | pubmed:dateCreated | 1991-11-8 | lld:pubmed |
| pubmed-article:1911857 | pubmed:abstractText | The effect of the anionic detergent sodium dodecyl sulfate (SDS) on human PAI-1 present in plasma, platelet extracts and endothelial cell cultures, was examined. Using the dye partitional extraction method of Mukerjee [1956) Anal. Chem. 28, 870-873) to quantitate ionic surfactants, and a discontinuous spectrophotometric assay for the titration of PAI-1 based on the measurement of residual active t-PA, we found (i) that SDS remains tightly bound to PAI-1 after equilibrium dialysis and (ii) that the activity of the latter was closely related to the amount of SDS carried over by the PAI-1 solution. The highest concentrations of SDS (ratio of SDS to protein greater than 0.1) were detected in the platelet-derived sources of PAI-1 which also showed the lowest residual t-PA activity. Moreover, it is demonstrated by SDS-PAGE and autoradiography that the tight binding of SDS to PAI-1 decreases its ability to form complexes with t-PA. Similar results were obtained with PAI-1 previously inactivated at 37 degrees C: the inability of PAI-1 to form complexes with t-PA was unchanged after SDS treatment. These observations suggest that the decrease in the residual activity of t-PA observed with the SDS-treated PAI-1 preparations is not related to an increase in the inhibitory activity of PAI-1. In fact, SDS was able to produce a decrease in both the binding of t-PA to fibrin and the activation of plasminogen by fibrin-bound t-PA. Bovine PAI-1 has been shown to exist in a latent SDS-activatable form. Our data indicate that such a form might not be present in the human sources of PAI-1 we have tested. | lld:pubmed |
| pubmed-article:1911857 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1911857 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1911857 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1911857 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1911857 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1911857 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1911857 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1911857 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1911857 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:1911857 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:1911857 | pubmed:author | pubmed-author:Anglés-CanoEE | lld:pubmed |
| pubmed-article:1911857 | pubmed:author | pubmed-author:GaussemPP | lld:pubmed |
| pubmed-article:1911857 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1911857 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:1911857 | pubmed:volume | 1079 | lld:pubmed |
| pubmed-article:1911857 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1911857 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1911857 | pubmed:pagination | 321-9 | lld:pubmed |
| pubmed-article:1911857 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
| pubmed-article:1911857 | pubmed:meshHeading | pubmed-meshheading:1911857-... | lld:pubmed |
| pubmed-article:1911857 | pubmed:meshHeading | pubmed-meshheading:1911857-... | lld:pubmed |
| pubmed-article:1911857 | pubmed:meshHeading | pubmed-meshheading:1911857-... | lld:pubmed |
| pubmed-article:1911857 | pubmed:meshHeading | pubmed-meshheading:1911857-... | lld:pubmed |
| pubmed-article:1911857 | pubmed:meshHeading | pubmed-meshheading:1911857-... | lld:pubmed |
| pubmed-article:1911857 | pubmed:meshHeading | pubmed-meshheading:1911857-... | lld:pubmed |
| pubmed-article:1911857 | pubmed:meshHeading | pubmed-meshheading:1911857-... | lld:pubmed |
| pubmed-article:1911857 | pubmed:meshHeading | pubmed-meshheading:1911857-... | lld:pubmed |
| pubmed-article:1911857 | pubmed:meshHeading | pubmed-meshheading:1911857-... | lld:pubmed |
| pubmed-article:1911857 | pubmed:meshHeading | pubmed-meshheading:1911857-... | lld:pubmed |
| pubmed-article:1911857 | pubmed:meshHeading | pubmed-meshheading:1911857-... | lld:pubmed |
| pubmed-article:1911857 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1911857 | pubmed:articleTitle | The formation of complexes between human plasminogen activator inhibitor-1 (PAI-1) and sodium dodecyl sulfate: possible implication in the functional properties of PAI-1. | lld:pubmed |
| pubmed-article:1911857 | pubmed:affiliation | Institut National de la Santé et de la Recherche Médicale, Hôpital de Bicêtre, France. | lld:pubmed |
| pubmed-article:1911857 | pubmed:publicationType | Journal Article | lld:pubmed |
