The enzymatic hydrolysis of 6-acylamino-4-methylumbelliferyl-beta-D-glucosides: identification of a novel human acid beta-glucosidase
Autor: | Margarita Mikhaylova, Valery Mikhaylov, Gherman Wiederschain, Johannes M. F. G. Aerts |
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Přispěvatelé: | Other departments, Faculteit der Geneeskunde |
Jazyk: | angličtina |
Rok vydání: | 1996 |
Předmět: |
Kidney
Isozyme Fluorogenic substrates Fluorescence Substrate Specificity chemistry.chemical_compound Glucosides Enzymatic hydrolysis Animals Humans Isoelectric Point Molecular Biology Human β-glucosidases chemistry.chemical_classification Gaucher Disease biology Hydrolysis beta-Glucosidase Fibroblasts Hydrogen-Ion Concentration Chromatography Agarose Rats Cytosol Isoelectric point Enzyme chemistry Biochemistry Liver Concanavalin A biology.protein Chromatography Gel Glucosylceramidase Molecular Medicine Beta-D Lysosomes Hymecromone Spleen Conduritol Subcellular Fractions |
Zdroj: | ResearcherID BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE, 1317(1), 71-79. Elsevier Biochimica et Biophysica Acta, 1317, 71-79 |
ISSN: | 0925-4439 0006-3002 |
Popis: | Fluorogenic 6-acylamino-4-methylumbelliferyl-beta-D-glucosides were found to be poor substrates for the three known human beta-glucosidases, i.e., lysosomal and non-lysosomal glucocerebrosidases and cytosolic broad-specificity beta-glucosidase. However, homogenates of human tissues and human cell types showed significant enzymatic hydrolysis of 6-ethanoylamino-4-methylumbelliferyl-beta-D-glucoside (EMGlc) due to the activity of a hitherto undescribed beta-glucosidase, called here EMGlc-ase. It was shown that the isozyme is hardly active towards 4-methylumbelliferyl-beta-D-glucoside or glucosylceramide. EMGlc-ase exhibits maximal activity at pH 4.5 and 5.0 in the absence and presence of sodium taurocholate respectively. It is a soluble lysosomal enzyme with a discrete isoelectric point of about 5.0. EMGlc-ase is not inhibited by conduritol B-epoxide, is activated by sodium taurocholate and binds strongly to Concanavalin A. This enzyme is not deficient in relation to Gaucher disease. |
Databáze: | OpenAIRE |
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