Thrombelastographic patterns of ancrod and thrombin fibrin formation and dissolution.

  title={Thrombelastographic patterns of ancrod and thrombin fibrin formation and dissolution.},
  author={Joseph Caprini and Hau C Kwaan and L. Zuckerman and Remi Verduin},
  journal={Thrombosis research},
  volume={4 2},
Abstract The dynamics of clot formation using either thrombin or arvin to clot purified human fibrinogen F XIII free fibrinogen and human plasma was studied using the thrombelastograph (TEG). Varying concentrations of these components including calcium were observed for their effects on the overall clotting patterns. The action of plasmin or urokinase on these systems was also evaluated. The production of equal area thrombelastographic tracings required over four times the amount of Ancrod… 
Structural origins of fibrin clot rheology.
Clot rigidity was enhanced by increasing fiber and branchpoint densities at greater fibrinogen concentrations, and network morphology is only minimally altered by the FXIIIa-catalyzed cross-linking reaction, which seems to augment clot rigidity most likely by the stiffening of existing fibers.
Reduction of brain injury by antithrombotic agent acutobin after middle cerebral artery ischemia/reperfusion in the hyperglycemic rat
It is indicated that acutobin improves brain tissue perfusion and reduces infarct volume and mortality in the hyperglycemic rat MCAO/R model.


Differences in the subunit structure of human fibrin formed by the action of arvin, reptilase and thrombin.
The fibrin formed by arvin seems to be more friable than that produced by thrombin or reptilase, which would explain why the fibrins produced by reptilases seem to bemore friable compared to those produced by other proteolytic enzymes.
The proteolytic action of Arvin on human fibrinogen.
Although Arvin is known to differ from ;reptilase' from Bothrops jararaca in that it does not activate the enzyme that cross-links fibrin (fibrin-stabilizing factor), it is identical with reptilase with respect to the peptides that it liberates from fibr inogen.
Studies on the activation of purified human factor XIII.
  • H. Tyler
  • Chemistry, Medicine
    Biochimica et biophysica acta
  • 1970
The ability of reptilase to activate Factor XIII supports this idea though another coagulant enzyme, Arvin, was ineffective, and Activation by thrombin may be the result of limited proteolysis somewhat analogous to that responsible for the fibr inogen to fibrin conversion.
Characterization of peptides released from human fibrinogen by Arvin.