Hementin
Direct fibrinogenolytic enzyme cleaving fibrinogen alpha-chain at unique sites — independent of plasmin.
Preclínico / mecanísticoLast updated: 2026-05-26 · Reviewed by ASH Editorial Board
Mechanistic Evidence Box
Preclinical / mechanistic- Page type
- Compound profile
- Evidence type
- Direct fibrinogenolytic enzyme cleaving fibrinogen alpha-chain at unique sites — independent of plasmin.
- Evidence level
- In vitro
- Drug vs leech
- Purified natural compound
- Safety domains
- Bleeding
Clinical translation limit
Hementin's in vitro fibrinogenolytic activity does not establish clinical efficacy as a thrombolytic. No FDA-approved derivative exists. Mechanism is preclinical/biochemical only.
Molecular Profile
- Category
- Fibrinolytic
- Evidence tier
- Preclinical
- Molecular weight
- 80,000 Da
- Source species
- Haementeria ghilianii (giant Amazon leech)
- Discovered
- 1984 · Malinconico, Budzynski et al.
Biological Targets
- → fibrinogen Aα and Bβ chains
Key Citations
- Malinconico SM et al. (1984), Thromb Res · PMID 6387015
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.
Destabilase Isopeptidase Activity
Isopeptidase domain of destabilase that cleaves cross-linked fibrin — distinct from lysozyme domain.
Destabilase-2
Second isoform of destabilase — lysozyme / isopeptidase activity targeting cross-linked fibrin.