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• W2000562124 abstract "Abstract Glycosidases modify, degrade and regulate glycoconjugates and are possibly involved in nutrition as well as in inflammation and humoral defense reactions in invertebrates. In this study, hemolymph from the freshwater snail Biomphalaria glabrata has been analyzed for its content of serum glycosidases by photometric assays and after protein separation by native-polyacrylamide gel electrophoresis and isolectric focusing. Activity of β- d -fucosidase, β- d -galactosidase, β- d -glucosidase, β- d -mannosidase, β- d -glucuronidase, N -acetyl-β- d -galactosaminidase, N -acetyl-β- d -glucosaminidase and lysozyme was detected. Highest enzyme activity corresponds to β- d -fucosidase followed by β- d -glucosidase > β- d -galactosidase > β- d -mannosidase > lysozyme > glucuronidase > hexosaminidase(s). Enzymes are active in the range of pH values between 3.5 and 7.5. The pH optima of the enzymes are between pH 3.5 and 6.5 (β- d -glucuronidase, N-acetyl-β- d -hexosaminidase(s):pH 3.5; lysozyme: pH 5.0; β- d -mannosidase: pH 5.5; β- d -fucosidase, β- d -galactosidase, β- d -glucosidase: pH 5.5–6.5). Molecular weights of native enzymes are between 90 and 460 kDa (β- d -glucuronidase, 430–460 kDa; β- d -fucosidase, β- d -galactosidase, α/β- d -glucosidase, 290–320 and 330–380 kDa; N -acetyl-β- d -hexosaminidase(s), 220–280 kDa; β- d -mannosidase, 185–290 kDa; α- d -mannosidase; 90–100 kDa)." @default.
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• W2000562124 date "1996-07-01" @default.
• W2000562124 modified "2023-09-26" @default.
• W2000562124 title "Detection and partial characterization of glycosidases in the hemolymph of Biomphalaria glabrata (Gastropoda)" @default.
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• W2000562124 doi "https://doi.org/10.1016/0305-0491(96)00020-x" @default.
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