Hirudinase
Alternate fibrin-cleaving enzyme reported in Hirudo medicinalis salivary secretions.
Preclinical / mechanisticLast updated: 2026-05-26 · Reviewed by ASH Editorial Board
Mechanistic Evidence Box
Preclinical / mechanistic- Page type
- Compound profile
- Evidence type
- Alternate fibrin-cleaving enzyme reported in Hirudo medicinalis salivary secretions.
- Evidence level
- Mechanistic discussion
- Drug vs leech
- Purified natural compound
- Safety domains
- Bleeding
Clinical translation limit
Hirudinase is documented mechanistically only; no human evidence. Reported fibrinolytic activity does NOT establish clinical thrombolytic efficacy, and no FDA-approved derivative exists.
Molecular Profile
- Category
- Fibrinolytic
- Evidence tier
- Preclinical
- Molecular weight
- 30,000 Da
- Source species
- Hirudo medicinalis
- Discovered
- 2009
Biological Targets
- → fibrin
- → fibrinogen
Key Citations
- Liu Z et al. (2019), Parasit Vectors
External Resources
Related Fibrinolytic Compounds
Destabilase
Lysozyme with isopeptidase activity that dissolves stabilized fibrin clots — including aged thrombi resistant to tPA.
Hementerin
Direct fibrinogenolytic enzyme — degrades fibrinogen independently of plasmin.
Hementin
Direct fibrinogenolytic enzyme cleaving fibrinogen alpha-chain at unique sites — independent of plasmin.
Destabilase Isopeptidase Activity
Isopeptidase domain of destabilase that cleaves cross-linked fibrin — distinct from lysozyme domain.