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http://purl.uniprot.org/citations/20600221http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20600221http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20600221http://www.w3.org/2000/01/rdf-schema#comment"A hemorrhagic metalloproteinase, named Batx-I, was isolated from the venom of Bothrops atrox specimens (from Southeastern Colombian region) by a combination of CM-Sephadex C25 ion-exchange and Affi-gel Blue affinity chromatographies. This enzyme accounts for about 45% of venom proteins, and it has an ESI-MS isotope-averaged molecular mass of 23296.2 Da and a blocked N-terminus. Two internal fragments sequenced by mass spectrometric analysis showed similarity to other SVMPs from Bothrops venoms. To investigate the possible participation of Batx-I in the envenomation pathophysiology, proteolytic, fibrinogenolytic, hemorrhagic, and other biological activities were evaluated. The minimal hemorrhagic dose obtained was 17 microg/20 g body weight. The enzyme showed proteolytic activity on azocasein, comparable with activity of BaP1. This activity was inhibited by EDTA and 1, 10 o-phenanthroline but not by aprotinin, pepstatin A or PMSF. Fibrinogenolytic activity was analyzed by SDS-PAGE, revealing a preference for degrading the A alpha- and B beta-chains, although partial degradation of the gamma-chain was also detected. The protein lacks coagulant and defibrinating activity. The CK levels obtained, clearly reflects a myotoxic activity induced by Batx-I. The hemorrhagic and fibrinogenolytic activities exhibited by the isolated PI-SVMP may play a role in the hemorrhagic and blood-clotting disorders observed in patients bitten by B. atrox in Colombia."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.org/dc/terms/identifier"doi:10.1016/j.toxicon.2010.06.016"xsd:string
http://purl.uniprot.org/citations/20600221http://purl.org/dc/terms/identifier"doi:10.1016/j.toxicon.2010.06.016"xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/author"Calvete J.J."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/author"Calvete J.J."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/author"Fernandez M."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/author"Fernandez M."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/author"Nunez V."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/author"Nunez V."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/author"Sanz L."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/author"Sanz L."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/author"Rucavado A."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/author"Rucavado A."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/author"Pereanez J.A."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/author"Pereanez J.A."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/author"Benjumea D.M."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/author"Benjumea D.M."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/author"Patino A.C."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/author"Patino A.C."xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/name"Toxicon"xsd:string
http://purl.uniprot.org/citations/20600221http://purl.uniprot.org/core/name"Toxicon"xsd:string