Sociedad Americana de Hirudoterapia

Leech Apyrase

ADP-degrading enzyme — prevents platelet aggregation by hydrolyzing ADP at bite site.

Preclínico / mecanísticoLast updated: 2026-05-26 · Reviewed by ASH Editorial Board
Molecular weight of Leech Apyrase 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 Leech Apyrase (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
ADP-degrading enzyme — prevents platelet aggregation by hydrolyzing ADP at bite site.
Evidence level
Mechanistic discussion
Drug vs leech
Leech-derived crude extract
Safety domains
Bleeding

Clinical translation limit

Leech apyrase's ADP-degrading mechanism is described at the bite site only and does not establish clinical antiplatelet efficacy. No FDA-approved derivative exists.

Molecular Profile

Category
Antiplatelet
Evidence tier
Preclinical
Molecular weight
67,000 Da
Source species
Hirudo medicinalis
Leech Apyrase molecular structure

Biological Targets

  • ADP (adenosine diphosphate)

External Resources

    Related Antiplatelet Compounds

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