rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2007-8-8
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pubmed:abstractText |
Streptokinase (SK) is a potent plasminogen activator with widespread clinical use as a thrombolytic agent. It is naturally secreted by several strains of beta-haemolytic streptococci. The low yields obtained in SK production, lack of developed gene transfer methodology and the pathogenesis of its natural host have been the principal reasons to search for a recombinant source for this important therapeutic protein. We report here the expression and secretion of SK by the Gram-positive bacterium Streptomyces lividans. The structural gene encoding SK was fused to the Streptomyces venezuelae CBS762.70 subtilisin inhibitor (vsi) signal sequence or to the Streptomyces lividans xylanase C (xlnC) signal sequence. The native Vsi protein is translocated via the Sec pathway while the native XlnC protein uses the twin-arginine translocation (Tat) pathway.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17610745-1011996,
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pubmed:language |
eng
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pubmed:journal |
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pubmed:status |
PubMed-not-MEDLINE
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pubmed:issn |
1475-2859
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20
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pubmed:dateRevised |
2009-11-18
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pubmed:year |
2007
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pubmed:articleTitle |
Recombinant production of Streptococcus equisimilis streptokinase by Streptomyces lividans.
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pubmed:affiliation |
Laboratorio de Genética, Departamento de Investigaciones Biomédicas, Centro de Química Farmacéutica, Ciudad de la Habana, Cuba. epimienta@infomed.sld.cu
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pubmed:publicationType |
Journal Article
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