Sociedad Americana de Hirudoterapia

Hementerin

Direct fibrinogenolytic enzyme — degrades fibrinogen independently of plasmin.

Preclínico / mecanísticoLast updated: 2026-05-26 · Reviewed by ASH Editorial Board
Molecular weight of Hementerin compared with other characterized leech-derived compoundsHementerin80 kDaHementin80 kDaHementin-Like Protein (HLP-1)80 kDaLeech Collagenase70 kDaHaemadipsa yanyuanensis Progr…70 kDaLeech Apyrase67 kDaCalin65 kDaHyaluronidase60 kDaAntithrombin III binding prot…58 kDaCollagenolytic Fibrinolysin55 kDaLeech Thrombospondin-Like Pro…50 kDaLHyal (Leech Hyaluronidase)50 kDa
Molecular weight (kilodaltons) of Hementerin (highlighted) alongside other characterized leech salivary compounds. Smaller proteins/peptides generally diffuse and act faster.

Mechanistic Evidence Box

Preclinical / mechanistic
Page type
Compound profile
Evidence type
Direct fibrinogenolytic enzyme — degrades fibrinogen independently of plasmin.
Evidence level
In vitro
Drug vs leech
Purified natural compound
Safety domains
Bleeding

Clinical translation limit

Hementerin's in vitro fibrinogenolytic activity does not establish clinical efficacy as a thrombolytic agent. 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 depressa
Discovered
1992 · Chudzinski-Tavassi et al.
Hementerin molecular structure

Biological Targets

  • fibrinogen Aα chain

Key Citations

  1. Chudzinski-Tavassi AM et al. (1998), Toxicon

External Resources

    Related Fibrinolytic Compounds

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