[Lysozyme activity of the salivary gland secretion of the medicinal leech H. verbana, H. medicinalis and H. orientalis].
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).
I P
IP
Baskova
O V
OV
Kharitonova
L L
LL
Zavalova
D000818:Animals; D010450:Endopeptidases / Q000378:metabolism; D047709:Hirudo medicinalis / Q000201:enzymology*; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D007865:Leeches / Q000201:enzymology*; D009113:Muramidase / Q000737:chemistry* / Q000302:isolation & purification; D010457:Peptidoglycan / Q000737:chemistry / Q000378:metabolism; D012463:Saliva / Q000201:enzymology*; D012469:Salivary Glands / Q000201:enzymology* / Q000378:metabolism; D013379:Substrate Specificity
D007527:Isoenzymes; D010457:Peptidoglycan; C421864:hen egg lysozyme; D009113:Muramidase; D010450:Endopeptidases; C045348:fibrin destabilase