Lysozyme activity of the salivary gland secretion of the medicinal leech H. verbana, H. medicinalis and H. orientalis
Basic science published in Biomed Khim (2011)
Abstract
Salivary gland secretions of three species of the medicinal leech differ in the level of lysozyme peptidoglycan-lysing activity. Using the synthetic fluorogenic substrate, 4-methyl-umbelliferyl tetra N-acetyl-beta-chitotetraosid, the glycosidase activity (as one of peptidoglycan-lysing activities) of salivary gland secretion of three species of the medicinal leech was quantitatively evaluated in comparison with egg lysozyme. It is supposed, that lysozyme activity of the leech secretions is determined not only by 5 isoforms of destabilase-lysozyme, but by some other enzymes which can utilize this substrate. These may be lysozymes other than i- (invertebrate) lysozymes (such as destabilase-lysozyme, or related enzymes).
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Zusammenfassung
Three medicinal leech species differ in salivary lysozyme peptidoglycan-lysing activity.
Warum dies für die Hirudotherapie relevant ist
This study quantitatively compared lysozyme peptidoglycan-lysing and glycosidase activities in salivary gland secretions of three species of the medicinal leech using a fluorogenic chitotetraoside substrate, finding interspecies differences and proposing that activity may reflect not only five isoforms of destabilase-lysozyme but also other, possibly non-i-type lysozymes. This is relevant to ASH's domain as a characterization of peptidoglycan-lysing components of leech salivary secretion across species. The caveat is that this is an in-vitro study of salivary gland secretion with no clinical data and no direct demonstration of therapeutic implications; interspecies differences may not translate to outcome differences in practice.
Zitation
Lysozyme activity of the salivary gland secretion of the medicinal leech H. verbana, H. medicinalis and H. orientalis.
Baskova IP et al. · Biomeditsinskaia khimiia, 2011
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