Highly active fractions of the medicinal leech recombinant destabilase-lysozyme
Research article published in 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.
Resumen
Highly active fractions of the medicinal leech recombinant destabilase-lysozyme.
Por qué esto importa para la hirudoterapia
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.
Citación
Highly active fractions of the medicinal leech recombinant destabilase-lysozyme
Fadeeva IY et al. · Biomeditsinskaia khimiia, 2014
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Añadido a la biblioteca ASH: May 27, 2026 · Última actualización del sitio: June 18, 2026