Production and evaluation of recombinant hirudin
Basic science / preclinical published in Seminars in thrombosis and hemostasis (1989)
Abstract
Hirudin, a 65 amino acid polypeptide form the medicinal leech, is an extremely efficient and specific thrombin inhibitor whose therapeutic potential has been demonstrated in a number of animal models. We have developed protocols for the production of recombinant hirudin by secretion from S. cerevisiae and carried out a full biologic evaluation of the purified product. These studies showed that natural and recombinant hirudin was similar in structure and in biologic function in vitro. Moreover, the recombinant protein displayed strong antithrombotic activity in several experimental thrombosis models in vivo, confirming the molecule's promise in the therapy of thrombotic disorders.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Summary
Hirudin, a 65 amino acid polypeptide form the medicinal leech, is an extremely efficient and specific thrombin inhibitor whose therapeutic potential has been demonstrated in a number of animal models.
Why This Matters for Hirudotherapy
This study examined protocols for producing recombinant hirudin—a 65 amino acid polypeptide from the medicinal leech that functions as a specific thrombin inhibitor—through secretion from S. cerevisiae, and evaluated the purified product against natural hirudin for structural similarity, in vitro biologic function, and in vivo antithrombotic activity in experimental thrombosis models. This work is relevant to hirudotherapy because hirudin is a leech-derived molecule with demonstrated therapeutic potential, and the finding that recombinant and natural forms are similar in structure and function supports biotechnological production as an alternative source of this antithrombotic agent. The scope is limited to the isolated hirudin molecule; it does not involve live leech therapy or other leech salivary components, and the in vivo antithrombotic activity was demonstrated in experimental animal models rather than human subjects.
Citation
Production and evaluation of recombinant hirudin.
Courtney M et al. · Seminars in thrombosis and hemostasis, 1989
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