| dc.creator | Pepe, Alfonso | |
| dc.creator | Frey, María Eugenia | |
| dc.creator | Muñoz, Fernando | |
| dc.creator | Fernández, María Belén | |
| dc.creator | Pedraza, Anabela | |
| dc.creator | Galbán, Gustavo | |
| dc.creator | García, Diana Noemí | |
| dc.creator | Daleo, Gustavo Raúl | |
| dc.creator | Guevara, María Gabriela | |
| dc.date | 2016-03-24 | |
| dc.date.accessioned | 2019-05-28T11:33:44Z | |
| dc.date.available | 2019-05-28T11:33:44Z | |
| dc.identifier | http://digital.cic.gba.gob.ar/handle/11746/5342 | |
| dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/2863839 | |
| dc.description | Plant 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.format | application/pdf | |
| dc.format | 8 p. | |
| dc.language | Inglés | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 International (BY-NC-ND 4.0) | |
| dc.subject | Biología Celular, Microbiología | |
| dc.title | Fibrin(ogen)olytic and antiplatelet activities of a subtilisin-like protease from Solanum tuberosum (StSBTc-3) | |
