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Related Experiment Video

Updated: May 11, 2026

High Throughput Quantitative Expression Screening and Purification Applied to Recombinant Disulfide-rich Venom Proteins Produced in E. coli
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Published on: July 30, 2014

Zinc-dependent prothrombin activator from Rhabdophis tigrinus venom with extended substrate specificity.

Noboru Inoue1, Yoshihiko Sakurai1, Kyoko Hasuwa1

  • 1Department of Legal Medicine, Nara Medical University, Kashihara, Nara, Japan.

Toxicon : Official Journal of the International Society on Toxinology
|March 2, 2026
PubMed
Summary

The Rhabdophis tigrinus snake

Keywords:
Blood coagulationMetalloproteaseProcoagulant activityProthrombin activatorRhabdophis tigrinusSnake venom metalloproteinase

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Published on: May 24, 2024

Area of Science:

  • Biochemistry
  • Toxicology
  • Enzymology

Background:

  • Rhabdophis tigrinus venom contains a potent prothrombin activator.
  • The enzyme's properties and classification were previously unknown.

Purpose of the Study:

  • To partially purify and characterize the prothrombin activator from R. tigrinus venom.
  • To determine its enzymatic and structural properties and classify the enzyme.

Main Methods:

  • Partial purification using gel filtration and hydroxyapatite chromatography.
  • SDS-PAGE, inhibitor studies, and LC/MS analysis.
  • Prothrombin activation assays using human plasma and synthetic peptides.

Main Results:

  • A disulfide-linked homodimer (approx. 110 kDa) was purified, termed Rhabdarin.
  • Rhabdarin is a zinc-dependent metalloprotease, not a serine protease.
  • It acts as a Group A prothrombin activator with sequence-context-dependent specificity.

Conclusions:

  • Rhabdarin is a novel zinc-dependent metalloprotease.
  • It represents a unique class of prothrombin activators with distinct substrate specificity.
  • Provides new insights into snake venom procoagulant enzyme evolution and classification.