Recombinant snake venom prothrombin activators

  title={Recombinant snake venom prothrombin activators},
  author={A. L{\"o}vgren},
  pages={153 - 157}
  • A. Lövgren
  • Published 2013
  • Biology, Medicine
  • Bioengineered
Three prothrombin activators; ecarin, which was originally isolated from the venom of the saw-scaled viper Echis carinatus, trocarin from the rough-scaled snake Tropidechis carinatus, and oscutarin from the Taipan snake Oxyuranus scutellatus, were expressed in mammalian cells with the purpose to obtain recombinant prothrombin activators that could be used to convert prothrombin to thrombin. We have previously reported that recombinant ecarin can efficiently generate thrombin without the need… Expand
5 Citations
Blood Coagulation Induced by Iranian Saw-Scaled Viper (Echis Carinatus) Venom: Identification, Purification and Characterization of a Prothrombin Activator
This study showed that the fraction which separated from Iranian snake Echis carinatus venom can be a prothrombin activators, and it can be concluded that this fraction is a procoagulant factor. Expand
Progress Curve Analysis of the One Stage Chromogenic Assay for Ecarin.
It is demonstrated here that rates of prothrombin and p-nitroaniline production can be converted to absolute thrombin concentrations using the Michaelis-Menten equation, substituted with values for kcat and Km. Expand
Snake Venoms in Drug Discovery: Valuable Therapeutic Tools for Life Saving
An up-to-date survey on the pharmacology of snake-venom bioactive components is shown and their therapeutic perspectives against a wide range of pathophysiological conditions are evaluated. Expand
Formulation adhésive et utilisations associées
La presente invention concerne une formulation adhesive qui comprend un melange contenant un fibrinogene et un activateur exogene d'un element d'une cascade de coagulation sanguine mammifere.


Prothrombin Activation by Snake Venom Proteases
This work has shown that metalloproteases that efficiently convert prothrombin into meizothrombin through the activation of serine proteases are also stimulated by negatively charged phospholipids and CaCl2 but not by factor Va. Expand
Two parallel prothrombin activator systems in Australian rough-scaled snake, Tropidechis carinatus. Structural comparison of venom prothrombin activator with blood coagulation factor X.
The present study confirms the presence of two separate genes--one each for FX and trocarin D, that code for similar proteins in T. carinatus snake, suggesting that snake venom prothrombin activators have probably evolved by the duplication of the liver FX gene and subsequently marked for tissue-specific expression in the venom gland. Expand
The intriguing world of prothrombin activators from snake venom.
  • R. Kini
  • Biology, Medicine
  • Toxicon : official journal of the International Society on Toxinology
  • 2005
This review provides a detailed description of the current knowledge on all prothrombin activators and highlights several intriguing questions that are yet to be answered. Expand
The determination of prothrombin using synthetic chromogenic substrates; choice of a suitable activator.
A linear relation was found between the prothrombin concentration and the amount of p-nitroanilides generated per unit of time and staphylocoagulase and the factor X a preparation give similar results. Expand
Structure of two genes encoding parallel prothrombin activators in Tropidechis carinatus snake: gene duplication and recruitment of factor X gene to the venom gland
This work presents the first molecular evidence for the recruitment of a duplicated gene for expression in venom glands by a simple insertion in T. carinatus, and named this segment as VERSE (Venom Recruitment/Switch Element). Expand
Expression and Characterization of Recombinant Ecarin
The snake venom protease ecarin from Echis carinatus was expressed in stable transfected CHO-S cells grown in animal component free cell culture medium. Recombinant ecarin (r-ecarin) was secretedExpand
The role of phospholipids and factor Va in the prothrombinase complex.
Both in the absence and presence of phospholipid but without factor Va, prethrombin 2 is the main product formed during the initial stages of steady state prothrom bin activation, and the Vmax of thrombin formation slightly increases when more phospholipsid is present in the authors' experiments and there is a considerable increase of the Km for prothROMbin at higher phospholIPid concentrations. Expand
An overview of the structure and function of thrombin.
The specificity of thrombin toward substrates and cofactors, as well as its spatiotemporal regulation by effectors and inhibitors, is directed by features of the molecule that distinguish it from relatively nonspecific serine proteases like trypsin. Expand
Incorporation of Factor Va into Prothrombinase Is Required for Coordinated Cleavage of Prothrombin by Factor Xa*
Data indicate that the interaction of factor Xa with the heavy chain of factor Va strongly influences the catalytic activity of the enzyme resulting in increased rates for both prothrombin-activating cleavages. Expand
The use of snake venom-derived compounds for new functional diagnostic test kits in the field of haemostasis.
  • Reto Schoni
  • Medicine
  • Pathophysiology of haemostasis and thrombosis
  • 2005
Pentapharm Ltd. has a long tradition of producing and proceeding snake venom components as APIs and tools in pharmaceutical and diagnostic applications, beginning with the snake venom-derived productExpand