Destabilase from the medicinal leech is a representative of a novel family of lysozymes
Basic science published in Biochim Biophys Acta (2000)
Abstract
Intrinsic lysozyme-like activity was demonstrated for destabilase from the medicinal leech supported by (1) high specific lysozyme activity of the highly purified destabilase, (2) specific inhibition of the lysozyme-like activity by anti-destabilase antibodies, and (3) appreciable lysozyme-like activity in insect cells infected with recombinant baculoviruses carrying cDNAs encoding different isoforms of destabilase. Several isoforms of destabilase constitute a protein family at least two members of which are characterized by lysozyme activity. The corresponding gene family implies an ancient evolutionary history of the genes although the function(s) of various lysozymes in the leech remains unclear. Differences in primary structures of the destabilase family members and members of known lysozyme families allow one to assign the former to a new family of lysozymes. New proteins homologous to destabilase were recently described for Caenorhabditis elegans and bivalve mollusks suggesting that the new lysozyme family can be widely distributed among invertebrates. It remains to be investigated whether the two enzymatic activities (isopeptidase and lysozyme-like) are attributes of one and the same protein.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Zusammenfassung
Highly purified destabilase shows specific lysozyme activity confirmed by anti-destabilase antibodies and baculovirus-recombinant isoforms; destabilase family assigned to a new lysozyme family widely distributed in invertebrates.
Warum dies für die Hirudotherapie relevant ist
This study demonstrated that destabilase, a protein from the medicinal leech, possesses intrinsic lysozyme-like activity, confirmed through purified enzyme assays, antibody inhibition, and recombinant expression of destabilase isoforms in insect cells. Multiple destabilase isoforms form a novel family of lysozymes distinct from known families, with homologs identified in Caenorhabditis elegans and bivalve mollusks. The study characterizes a leech-derived protein with enzymatic activity of potential interest to ASH's domain. However, the work is purely biochemical and molecular in nature, does not involve hirudotherapy or clinical application, and the biological function of these lysozymes in the leech remains undetermined per the abstract.
Zitation
Destabilase from the medicinal leech is a representative of a novel family of lysozymes.
Zavalova LL et al. · Biochimica et biophysica acta, 2000
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