On the isolation of the thrombin inhibitor hirudin
Research article published in Thromb Res (1985)
Abstract
A procedure for isolation of hirudin from crude preparations was described. By the use of ion exchange chromatography and affinity chromatography preparations were obtained with a specific activity of 10 to 15 antithrombin units/micrograms. Separation into several fractions with the same activity suggests the existence of isoinhibitors.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Summary
Procedure for hirudin isolation from crude preparations using ion exchange and affinity chromatography; specific activity of 10-15 antithrombin units/microgram with separation into multiple isoinhibitors.
Why This Matters for Hirudotherapy
This article describes a laboratory procedure for isolating hirudin from crude preparations using ion exchange and affinity chromatography, achieving specific activities of 10–15 antithrombin units per microgram. Separation yielded several fractions with equivalent activity, leading the authors to suggest the existence of isoinhibitors. This work is relevant to ASH's domain only in the narrow biochemical sense of hirudin purification and the structural diversity of its active forms. The abstract provides no clinical, in-vivo, or therapeutic data, does not mention leeches, and its relevance is limited to methodology and biochemical characterization.
Citation
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