http://rdf.ncbi.nlm.nih.gov/pubchem/patent/BR-PI0200269-B1

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filingDate 2002-01-31-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_97e42e9a025042df21f85e72383fd83d
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_047335784d54bcbda65aa033a8a70f7d
publicationDate 2016-07-26-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber BR-PI0200269-B1
titleOfInvention process of purification of soluble proteins from l. obliqua with prothrombin activating activity and use of protein fraction
abstract "process of purification of soluble proteins of l. obliqua bristles with prothrombin activating activity; process for partial determination of prothrombin activator amino acid sequence; process of determining prothrombin activating activity of fraction ii, n-terminal sequence and sequence" of internal fragments of the prothrombin activating fraction, prothrombin activator and use of the prothrombin activator ". The present invention relates to a process for purifying soluble proteins from the bristles. oblique with prothrombin activating activity; the process for partial determination of the prothrombin activator amino acid sequence; the process of determining the prothrombin activating activity of fraction ii as well as the n-terminal sequence and sequence of internal fragments of the prothrombin activating fraction to the prothrombin activator and the use of the prothrombin activator starting from the homogenization of l bristles. oblique. The present invention proves that a single component of the Lonomia obliqua venom, lopap, causes the hemorrhagic syndrome directly by the activation of prothrombin and, therefore, should refer a therapy in the case of accidents with Lonomia obliqua. According to the present invention lopap is a new prothrombin activator, which is an important factor responsible for the consumption coagulopathy found in l-poisoned patients. oblique. In low doses the purified protein, due to its ability to activate prothrombin generating thrombin, withdraws fibrinogen from the circulation, transforming it into fibrin microcoagles. This decrease in fibrinogen plasma concentration allows the blood clotting time to extend and thus prevents acute vascular thrombosis. Because it has no proteolytic activity, the protein would maintain the coagulant capacity of fibrinogen not consumed in the process. thus the plasma concentration of fibrinogen would be decreased, but there would be no predisposition to a hemorrhagic state. In addition, it could be used in the manufacture of diagnostic kits for detection of plasma prothrombin.
priorityDate 2002-01-31-04:00^^<http://www.w3.org/2001/XMLSchema#date>
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