American Society of Hirudotherapy

Leech Apyrase

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

Preclinical / mechanisticLast 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

    This website provides educational information and does not constitute medical advice, diagnosis, or treatment recommendations. Medicinal leech therapy carries clinically meaningful risks and should be performed only by qualified clinicians under institutionally approved protocols. FDA 510(k) clearance for medicinal leeches is limited to specific indications; investigational and off-label discussions are labeled accordingly. For patient-specific guidance, consult a qualified healthcare provider.