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  3. Comisión de Investigaciones Científicas de la Prov. de Buenos Aires
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dc.provenanceComisión de Investigaciones Científicas-
dc.contributorPepe, Alfonso-
dc.contributorFrey, María Eugenia-
dc.contributorMuñoz, Fernando-
dc.contributorFernández, María Belén-
dc.contributorPedraza, Anabela-
dc.contributorGalbán, Gustavo-
dc.contributorGarcía, Diana Noemí-
dc.contributorDaleo, Gustavo Raúl-
dc.contributorGuevara, María Gabriela-
dc.creatorPepe, Alfonso-
dc.creatorFrey, María Eugenia-
dc.creatorMuñoz, Fernando-
dc.creatorFernández, María Belén-
dc.creatorPedraza, Anabela-
dc.creatorGalbán, Gustavo-
dc.creatorGarcía, Diana Noemí-
dc.creatorDaleo, Gustavo Raúl-
dc.creatorGuevara, María Gabriela-
dc.date2016-03-24-
dc.date.accessioned2019-04-29T16:12:13Z-
dc.date.available2019-04-29T16:12:13Z-
dc.date.issued2016-03-24-
dc.identifierhttp://digital.cic.gba.gob.ar/handle/11746/5342-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/311558-
dc.descriptionPlant serine proteases have been widely used in food science and technology as well as in medicine. In this sense, several plant serine proteases have been proposed as potential anti-coagulants and antiplatelet agents. Previously, we have reported the purification and identification of a plant serine protease from Solanum tuberosum leaves. This potato enzyme, named as StSBTc-3, has a molecular weight of 72 kDa and it was characterized as a subtilisin like protease. In this work we determine and characterize the biochemical and medicinal properties of StSBTc-3. Results obtained show that, like the reported to other plant serine proteases, StSBTc-3 is able to degrade all chains of human fibrinogen and to produces fibrin clot lysis in a dose dependent manner. The enzyme efficiently hydrolyzes b subunit followed by partially hydrolyzed a and g subunits of human fibrinogen. Assays performed to determine StSBTc-3 substrate specificity using oxidized insulin b-chain as substrate, show seven cleavage sites: Asn3-Gln4; Cys7-Gly8; Glu13-Ala14; Leu15-Tyr16; Tyr16-Leu17; Arg22-Gly23 and Phe25-Tyr26, all of them were previously reported for other serine proteases with fibrinogenolytic activity. The maximum StSBTc-3 fibrinogenolytic activity was determined at pH 8.0 and at 37 C. Additionally, we demonstrate that StSBTc- 3 is able to inhibit platelet aggregation and is unable to exert cytotoxic activity on human erythrocytes in vitro at all concentrations assayed. These results suggest that StSBTc-3 could be evaluated as a new agent to be used in the treatment of thromboembolic disorders such as strokes, pulmonary embolism and deep vein thrombosis.-
dc.formatapplication/pdf-
dc.format8 p.-
dc.languageeng-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International (BY-NC-ND 4.0)-
dc.sourcereponame:CIC Digital (CICBA)-
dc.sourceinstname:Comisión de Investigaciones Científicas de la Provincia de Buenos Aires-
dc.sourceinstacron:CICBA-
dc.source.urihttp://digital.cic.gba.gob.ar/handle/11746/5342-
dc.subjectBiología Celular, Microbiología-
dc.titleFibrin(ogen)olytic and antiplatelet activities of a subtilisin-like protease from Solanum tuberosum (StSBTc-3)-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/submittedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
Aparece en las colecciones: Comisión de Investigaciones Científicas de la Prov. de Buenos Aires

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