Isolation and structural characterization of a potent inhibitor of coagulation factor Xa from the leech Haementeria ghilianii

The present work reports the discovery and characterization of an anticoagulant protein in the salivary gland of the giant bloodsucking leech, H. ghilianii, which is a specific and potent inhibitor of coagulation factor Xa. The inhibitor, purified to homogeneity, displayed subnanomolar inhibition of bovine factor Xa and had a molecular weight of approximately 15,000 as deduced by denaturing SDS-PAGE. The amino acid sequence of the first 43 residues of the H. ghilianii derived inhibitor displayed a striking homology to antistasin, the recently described subnanomolar inhibitor of factor Xa isolated from the Mexican leech, H. officinalis. Antisera prepared to antistasin cross-reacted with the H. ghilianii protein in Western Blot analysis. These data indicate that the giant Amazonian leech, H. ghilianii, and the smaller Mexican leech, H. officinalis, have similar proteins which disrupt the normal hemostatic clotting mechanisms in their mammalian host's blood.

Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.

Isolation and structural characterization of a potent inhibitor of coagulation factor Xa from the leech Haementeria ghilianii.

Leech-derived molecules this paper discusses, each with a full profile in the ASH compound registry:

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