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Related Experiment Videos

Defibrinogenation by batroxobin and acylated batroxobin in rats.

M Richter1, M Paintz, J Stürzebecher

  • 1Institute of Pharmacology and Toxicology, Medical Academy, Erfurt, GDR.

Folia Haematologica (Leipzig, Germany : 1928)
|January 1, 1988
PubMed
Summary

Acylating batroxobin, a snake venom enzyme, creates benzoyl-batroxobin. This inactive form, upon deacylation, restores clotting activity and reduces microthrombosis risk in rats.

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Area of Science:

  • Biochemistry
  • Pharmacology
  • Toxicology

Background:

  • Batroxobin is a thrombin-like enzyme found in snake venom.
  • Snake venom enzymes have potential applications in medicine, but their activity needs careful control.

Purpose of the Study:

  • To investigate the acylation of batroxobin with 4-amidinophenyl benzoate.
  • To evaluate the enzymatic activity, deacylation kinetics, and in vivo effects of the modified enzyme, benzoyl-batroxobin.

Main Methods:

  • Acylation of batroxobin at the active site serine hydroxyl with 4-amidinophenyl benzoate.
  • Determination of deacylation half-life and recovery of clotting activity in plasma.
  • Intravenous injection of batroxobin and benzoyl-batroxobin in rats to assess defibrinogenation and microthrombosis.

Main Results:

  • Acylation yielded enzymatically inactive benzoyl-batroxobin.
  • Batroxobin activity was recovered with a deacylation half-life of approximately 1 hour.
  • Benzoyl-batroxobin showed retarded defibrinogenation compared to batroxobin and did not induce initial microthrombosis in rats.

Conclusions:

  • Acylation provides a method to temporarily inactivate batroxobin.
  • Benzoyl-batroxobin offers a potentially safer alternative for applications requiring controlled defibrinogenation due to its delayed action and reduced thrombotic potential.

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