| purification and characterization of a prothrombin activator from the venom of the australian brown snake, pseudonaja textilis textilis. | a simple procedure, involving chromatography on concanavalin a-sepharose and gel filtration, has been developed for the purification of a prothrombin activator from the venom of the australian brown snake pseudonaja textilis textilis. the prothrombin activator, which is a major venom component, is a high molecular weight protein (mr greater than or equal to 200,000) which yields a number of subunits when examined by sds-page. it is related antigenically to the venom prothrombin activator of the ... | 1988 | 3075905 |
| a family of textilinin genes, two of which encode proteins with antihaemorrhagic properties. | two peptides, textilinins 1 and 2, isolated from the venom of the australian common brown snake, pseudonaja textilis textilis, are effective in preventing blood loss. to further investigate the potential of textilinins as antihaemorrhagic agents, we cloned cdnas encoding these proteins. the isolated full-length cdna (430 bp in size) was shown to code for a 59 amino acid protein, corresponding in size to the native peptide, plus an additional 24 amino acid propeptide. six such cdnas were identifi ... | 2002 | 12406072 |
| crystallization and preliminary x-ray analysis of a kunitz-type inhibitor, textilinin-1 from pseudonaja textilis textilis. | textilinin-1 (txln-1), a kunitz-type serine protease inhibitor, is a 59-amino-acid polypeptide isolated from the venom of the australian common brown snake pseudonaja textilis textilis. this molecule has been suggested as an alternative to aprotinin, also a kunitz-type serine protease inhibitor, for use as an anti-bleeding agent in surgical procedures. txln-1 shares only 47% amino-acid identity to aprotinin; however, six cysteine residues in the two peptides are in conserved locations. it is the ... | 2006 | 16820682 |
| hemostatic properties of a venomic protein in rodent dermal injuries. | hemostatic properties of a factor xa-like protease (q8009) from the australian snake pseudonaja textilis textilis were determined. in tail-tip transection and dermal incision (hind limb) models, reagents were applied with collagen matrix. blood was collected on filter paper chads for 12 one-minute intervals or until hemostasis. determination of blood loss was performed using the hematin content and reported as blood loss per minute and total blood lost. results from the studies demonstrated that ... | 2007 | 17574547 |
| hemostatic properties of a venomic protein in rat organ trauma. | previous in vitro work characterized the protease q8009 isolated from the venom of the australian brown snake pseudonaja textilis textilis with factor xa-like activity and hemostatic properties. the purpose of the work described here characterizes the in vivo hemostatic properties in a rat model of parenchymatous organ injury. the key parameters of activity included reduction in time-to-hemostasis and total volume of blood loss in spleen, liver and kidney wound models in rats. the surgical proto ... | 2009 | 19747909 |
| textilinins from pseudonaja textilis textilis. characterization of two plasmin inhibitors that reduce bleeding in an animal model. | the incidence of vein-graft occlusion associated with myocardial infarction and thrombosis following the use of the plasmin inhibitor, aprotinin, to reduce blood loss during vascular surgery has prompted the isolation of an alternative kinetically distinct inhibitor of plasmin from the venom of pseudonaja textilis. this inhibitor has been called textilinin (txln) and two distinct forms have been isolated from the brown-snake venom (molecular weight, 6688 and 6692). a comparison of plasmin inhibi ... | 2000 | 10847427 |
| comparison of active venom components between eastern brown snakes collected from south australia and queensland. | the abundance and activity of the prothrombin activator (pseutarin c) within the venom of the eastern brown snake (pseudonaja textilis textilis) is the primary determinant of its coagulation potency. textilinin-1, also in this venom, is a plasmin inhibitor which is thought to exert its toxic effects through the slowing of fibrinolysis. the aim of this report is to determine if there are differences in the potency of the venom from eastern brown snakes collected from south australia (sa) compared ... | 2006 | 16374664 |
| fibrinolysis as a feature of disseminated intravascular coagulation (dic) after pseudonaja textilis textilis envenomation. | blood was obtained from four patients envenomated by the australian common brown snake, pseudonaja textilis textilis. this elapid snake has one of the most toxic venoms in the world, containing extremely potent neurotoxic and coagulant components. the latter is a potent complete prothrombinase, converting prothrombin to alpha-thrombin, and comprises more than 30% of the total venom protein. the four envenomated patients developed a typical consumption coagulopathy. serial serum and plasma sample ... | 1990 | 2237840 |