[Glycosidases of various mollusks: general properties, kinetic studies and action on natural substrates].
The beta-N-acetylhexosaminidase, beta-glucuronidase, alpha-galactosidase, beta-galactosidase and alpha-L-fucosidase activities, in six different species of molluscs, have been studied. The optimum pH was acid in all cases, in agreement with the lysosomal origin of these enzymes. They generally show several pI in their isoelectrofocusing profiles. Kinetic studies with enzymes having several activities in one protein, i.e. beta-N-acetylhexosaminidase and beta-galactosidase, have been carried out with mixed substrates in order to determine the occurrence of several active sites. The action of these enzymes on glycosidic rests containing natural substrates has been studied by enzymatic hydrolysis.
D000818:Animals; D005966:Glucuronidase / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006596:Hexosaminidases / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007700:Kinetics; D008974:Mollusca / Q000201:enzymology*; D013045:Species Specificity; D013379:Substrate Specificity; D000519:alpha-Galactosidase / Q000378:metabolism; D005644:alpha-L-Fucosidase / Q000378:metabolism; D001616:beta-Galactosidase / Q000378:metabolism; D001619:beta-N-Acetylhexosaminidases
D006026:Glycoside Hydrolases; D006596:Hexosaminidases; D000519:alpha-Galactosidase; D001616:beta-Galactosidase; D005966:Glucuronidase; D005644:alpha-L-Fucosidase; D001619:beta-N-Acetylhexosaminidases
Glicosidasas de algunos moluscos: propiedades generales, estudios cinéticos y acción sobre substratos naturales.