Amino acid sequence of trocarin, a prothrombin activator from Tropidechis carinatus venom: its structural similarity to coagulation factor Xa.

@article{Joseph1999AminoAS,
  title={Amino acid sequence of trocarin, a prothrombin activator from Tropidechis carinatus venom: its structural similarity to coagulation factor Xa.},
  author={J. Joseph and M. Chung and K. Jeyaseelan and R. Kini},
  journal={Blood},
  year={1999},
  volume={94 2},
  pages={
          621-31
        }
}
Among snake venom procoagulant proteins, group II prothrombin activators are functionally similar to blood coagulation factor Xa. We have purified and partially characterized the enzymatic properties of trocarin, the group II prothrombin activator from the venom of the Australian elapid, Tropidechis carinatus (rough-scaled snake). Prothrombin activation by trocarin is enhanced by Ca2+, phospholipids, and factor Va, similar to that by factor Xa. However, its amidolytic activity on peptide… Expand
Group D prothrombin activators from snake venom are structural homologues of mammalian blood coagulation factor Xa.
TLDR
The purification of Group D prothrombin activators from three Australian snake venoms using a single-step method and their N-terminal sequences reveal that hopsarin D is structurally and functionally similar to mammalian coagulation FXa. Expand
Pseutarin C, a prothrombin activator from Pseudonaja textilis venom: its structural and functional similarity to mammalian coagulation factor Xa-Va complex.
Several snake venoms contain procoagulant proteins that can activate prothrombin. We have purified pseutarin C, a prothrombin activator from the venom of the Australian brown snake (PseudonajaExpand
The nonenzymatic subunit of pseutarin C, a prothrombin activator from eastern brown snake (Pseudonaja textilis) venom, shows structural similarity to mammalian coagulation factor V.
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The data demonstrate that the nonenzymatic subunit of group C prothrombin activators is structurally similar to mammalian FV. Expand
Gene Structures of Trocarin D and Coagulation Factor X, Two Functionally Diverse Prothrombin Activators from Australian Rough Scaled Snake
TLDR
The gene structure of Trocarin D and factor X, a venom prothrombin activator system in Australian rough scaled snake, is determined and it is shown that they share a very high degree of sequence identity indicating that the gene duplication is a recent event. Expand
The catalytic subunit of pseutarin C, a group C prothrombin activator from the venom of Pseudonaja textilis, is structurally similar to mammalian blood coagulation factor Xa.
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This is the first sequence of the catalytic subunit of a group C prothrombin activator of pseutarin C, a large protein complex consisting of catalytic and nonenzymatic subunits, which are functionally similar to the mammalian FXa-FVa complex. Expand
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Comparative analysis of prothrombin activators from the venom of Australian elapids.
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Cloning and functional expression of venom prothrombin activator protease from Pseudonaja textilis with whole blood procoagulant activity
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Trocarin, a blood coagulation factor Xa homologue from snake venom, causes inflammation and mitogenesis.
TLDR
It is shown that trocarin also causes edema in the mouse footpad; the inflammation, accompanied by a large purplish clot, is more persistent than the transient edema caused by FXa. Expand
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Basparin A is likely to play an important role in the coagulopathy associated with B. asper envenoming, and activity is completely inhibited by Costa Rican polyvalent (Crotalinae) anti-venom. Expand
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