American Society of Hirudotherapy

Highly active fractions of the medicinal leech recombinant destabilase-lysozyme

Research article published in Biomeditsinskaia khimiia (2014)

Last Updated: June 18, 2026Reviewed by: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: In vitro / laboratoryDrug DevelopmentFadeeva IY et al. · Biomeditsinskaia khimiia, 2014

Abstract

From the highly purified but lowly active recombinant protein Destabilas-Lysozyme (Dest-Lys) by use cation-exchange column TSK CM 3-SW chromatography, it was separated non-active fraction IV, contained 90% of protein. Fractions I, II and III, represented proteins with lysozyme and isopeptidase activities. Their lysozyme activity correlates with the activity of natural Des-Lys. The ratio of the activities in fractions I - III is such, that maximal lysozyme activity is concentrated in fraction III, isopeptidase - in fraction I. It is discussed the possibility of Dest-Lys different functions regulation is depended on the formation of protein complex forms. V rezul'tate fraktsionirovaniia vysokoochishchennogo nizkoaktivnogo rekombinantnogo belka destabilazy-lizotsima (Dest-Liz) na kationoobmennoĭ kolonke TSK CM 3-SW udalos' otdelit' neaktivnuiu fr.IV, soderzhashchuiu 90% belka, ot trekh fraktsiĭ (I, II i III), predstavliaiushchikh belki, lizotsimnaia i izopeptidaznaia aktivnosti kotorykh korreliruiut s aktivnostiami nativnogo fermenta. Odnako, sootnoshenie lizotsimnoĭ i izopeptidaznoĭ aktivnosteĭ vo fraktsiiakh I – III takovo, chto maksimal'naia lizotsimnaia aktivnost' sosredotochena vo fraktsii III, a izopeptidaznaia – vo fraktsii I. Obsuzhdaetsia vozmozhnost' reguliatsii raznykh funktsiĭ Dest-Liz v sviazi s obrazovaniem ego kompleksnykh form.

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

Publication typeEnglish AbstractJournal Article
Indexed MeSH termsAnimalsCarbon-Nitrogen LyasesChromatography, Ion ExchangeEndopeptidasesFibrinolytic AgentsHirudo medicinalisKineticsMuramidaseRecombinant ProteinsSubstrate Specificity

Summary

Highly active fractions of the medicinal leech recombinant destabilase-lysozyme.

Why This Matters for Hirudotherapy

This study describes chromatographic separation of recombinant destabilase-lysozyme (Dest-Lys) using a cation-exchange column, yielding three active fractions (I, II, III) with lysozyme and isopeptidase activities and one inactive fraction (IV, 90% of protein). Maximal lysozyme activity concentrated in fraction III while maximal isopeptidase activity was in fraction I, and the authors discussed whether regulation of Dest-Lys's different functions depends on formation of protein complex forms. Caveat: The abstract does not specify the source organism, describe the protein as part of a secretome, or characterize isopeptidase activity as fibrinolytic. While MeSH terms reference Hirudo medicinalis, the abstract itself does not establish a leech connection, so relevance to ASH's domain is indirect and cannot be confirmed from the abstract alone.

Citation

Highly active fractions of the medicinal leech recombinant destabilase-lysozyme

Fadeeva IY et al. · Biomeditsinskaia khimiia, 2014

DOI

Added to ASH library: May 27, 2026 · Site last updated: June 18, 2026

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.