Separation of monomerizing and lysozyme activities of destabilase from medicinal leech salivary gland secretion

Destabilase, endo-epsilon-(gamma-Glu)-Lys-isopeptidase, was prepared from the salivary gland secretion of the medicinal leech (Hirudo medicinalis). The secretion prepared by the known method of Rigbi et al. (1987) (secretion-K) lacks the destabilase-characteristic highly specific isopeptidase activity (the D-dimer-monomerizing activity) because of its degradation by proteolytic activity (the substrate of Glp-Ala-Ala-Leu-pNA) due to contamination with leech intestinal channel contents. Therefore, we have elaborated a new technique for preparation of a true leech secretion (secretion-I). This secretion is characterized by the complete absence of the leech intestinal channel contents and has no proteolytic activity. For the first time the destabilase-specific D-dimer-monomerizing and lysozyme activities were separated by fractionation of secretion-I by HPLC gel filtration through Superose S-12. For the purified destabilase preparation, these activities were separated by reversed-phase chromatography in an acetonitrile gradient (0-60%) in the presence of 0.1% trifluoroacetic acid. The monomerizing activity of destabilase is responsible for the ability of secretion-I to dissolve stabilized fibrin via isopeptidolysis of alpha-alpha and gamma-gamma fibrin chains bound by epsilon-(gamma-Glu)-Lys-isopeptide bonds.

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

Secretion-I free of intestinal contaminants enables HPLC separation of destabilase's monomerizing (D-dimer cleavage) and lysozyme activities, clarifying dual-functional mechanism.

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

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