Protein C Activators from Snake Venoms and Their Diagnostic Use

@article{GempelerMessina2001ProteinCA,
  title={Protein C Activators from Snake Venoms and Their Diagnostic Use},
  author={P. M. Gempeler-Messina and K W Volź and Beatrice B{\"u}hler and Ch. M{\"u}ller},
  journal={Pathophysiology of Haemostasis and Thrombosis},
  year={2001},
  volume={31},
  pages={266 - 272}
}
Proteinases converting the zymogen protein C (PC) of vertebrates into activated PC have been detected in several snake venoms. Most PC activators have been purified from venom of snake species belonging to the genera of the Agkistrodon complex. Unlike the physiological, thrombin-catalyzed PC activation reaction which requires thrombomodulin as a cofactor, most snake venom activators directly convert the zymogen PC into the catalytically active form which can easily be determined by means of… Expand
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References

SHOWING 1-10 OF 45 REFERENCES
Identification of protein c activator from nine species of Chinese snake venoms
AIM:To determine which species of snake venoms contained protein c activator among 9 species of Chinese snake venoms. METHODS: Anticoagulant activity was examined by activated partial thromboplastinExpand
Protein C activators in snake venoms.
TLDR
The use of Protac in quantitative PC determination bears significant advantages over the use of thrombin as an activator and in rabbits, i.v. injection ofProtac caused a prolonged APTT and did not provoke acute toxic reactions. Expand
Practical application of the protein C activator Protac from Agkistrodon contortrix venom.
The protein C activator Protac from A. contortrix venom is being investigated as a potential antithrombotic agent and as a tool for the preparation of activated protein C. Its established majorExpand
Characterization of the protein C activator Protac from the venom of the southern copperhead (Agkistrodon contortrix) snake.
TLDR
Conversion of the zymogen protein C into the active proteinase was demonstrated by measuring the prolongation of the activated partial thromboplastin time due to proteolytic degradation of factors Va and VIIIa by the activation product, as well as by direct measurement of the generated enzyme activity by means of a synthetic chromogenic substrate. Expand
Inhibition of the protein C activator Protac, a serine proteinase from the venom of the southern copperhead snake Agkistrodon contortrix contortrix.
TLDR
The active site of ProtacR appears to be accessible only for inhibitors with well-fitting structural features, and only a few 4-amidinoanilides of N alpha-substituted omega-phenyl-alpha-aminoalkylcarboxylic acids exert potent inhibitory activities. Expand
Purification of a protein C activator from the venom of the southern copperhead snake (Agkistrodon contortrix contortrix).
TLDR
The results suggest that the venom of the Southern copperhead snake contains a protease that is a specific activator of protein C, which can activate the vitamin K dependent protein, protein C. Expand
Isolation of a protein C activator from southern copperhead venom.
TLDR
A protease from the venom of the Southern Copperhead snake that activates protein C was purified to homogeneity by a combination of sulfopropyl (SP)-Sephadex C-50, SephadeX G-150 and Mono-S column chromatography to prolonged the clotting time of human plasma in a dose- and temperature-dependent manner. Expand
Isolation and characterization of a protein C activator from tropical moccasin venom.
TLDR
A protease from the venom of the tropical moccasin that activates protein C was purified to homogeneity by ion-exchange and gel permeation chromatography and Amino-terminal sequence analysis revealed that the tropicalmoccasin protein C activator was highly homologous to the protein C Activator isolated from Southern copperhead venom. Expand
Characterization of a protein C activator from the venom of Agkistrodon contortrix contortrix.
TLDR
The results suggest that the enzyme purified 60-fold from the venom of the Southern copperhead snake is a serine protease, which appears to be thrombin-like in its preference for arginyl as compared to lysyl chloromethyl ketones as well as by its inhibition by benzamidine and p-aminobenzamidine. Expand
[Antithrombotic effect of protein C activator from a snake venom].
TLDR
The effects of the activator observed appear to occur via transformation of the endogenous protein C into its active form, which prevents animal death when thrombosis was induced by means of administration of theThromboplastin lethal dose. Expand
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