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Biochimica et Biophysica Acta (BBA) - Biomembranes, 1993
The influence of phosphatidylserine (PS) liposome size on their capacity to activate and bind purified glucosylceramidase was investigated. Gel filtration and flotation experiments showed that large unilamellar vesicles (LUV) of either pure PS or PS in admixture with phosphatidylcholine (PC) are unable to tightly bind purified glucosylceramidase, and ...
A. M. Vaccaro +5 more
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The influence of phosphatidylserine (PS) liposome size on their capacity to activate and bind purified glucosylceramidase was investigated. Gel filtration and flotation experiments showed that large unilamellar vesicles (LUV) of either pure PS or PS in admixture with phosphatidylcholine (PC) are unable to tightly bind purified glucosylceramidase, and ...
A. M. Vaccaro +5 more
semanticscholar +3 more sources
Reconstitution of glucosylceramidase on binding to acidic phospholipid-containing vesicles
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992Studies were conducted to investigate the mechanism by which acidic phospholipid-containing vesicles stimulate purified placental glucosylceramidase activity towards the water-soluble substrate 4-methylumbelliferyl-beta-D-glucopyranoside (MUGlc). Vesicles composed of pure phosphatidic acid (PA) or pure phosphatidylserine (PS) stimulated the activity of
A M, Vaccaro +4 more
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Comparison of synthetic and natural glucosylceramides as substrate for glucosylceramidase assay.
Clinica Chimica Acta, 1982Commercially available [3H]glucosylceramide is derived from spleen tissue of patients with Gaucher's disease. When such tritiated glucosylceramide was diluted with unlabelled glucosylceramide from different sources and used as the substrate for assays of glucosylceramidase, the apparent activities obtained differed drastically.
Vacca Maria +2 more
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Factors Affecting the Binding of Glucosylceramidase to ItsNatural Substrate Dispersion
Enzyme, 1989 This paper reports the results of ultracentrifugation experiments devised for investigating the interactions occurring in the conditions of the enzymatic assay between glucosylceramidase and the components of the substrate dispersion. This dispersion contains, besides glucosylceramide, taurocholate and oleic acid.
Anna Maria Vaccaro +3 more
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Intracellular Activity of Lysosomal Glucosylceramidase Measured with 4-Nonylumbelliferyl β-glucoside
Biological Chemistry Hoppe-Seyler, 1989 Enzymatic activity of lysosomal glucosyl-ceramidase was determined in intact murine hybridoma and macrophage cells with the synthetic substrate nonylumbeliferyl-beta-glucoside (NUG). The substrate was applied as complex with bovine serum albumin (two binding sites, Kd 2.2 +/- 0.3 microM).
Erhard Bieberich, G. Legler
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Etiology of a New Identified Gaucher Disease Variant without Glucosylceramidase Defect
, 1988 Gaucher disease, the most prevalent lysosomal storage disease, is a group of autosomal recessively inherited disorders characterized by the accumulation of glucosylceramide in lysosomes of the cells of the reticuloendothelial system. This sphingolipidosis is caused by the hereditary deficiency of the membran associated lysosomal enzyme β ...
Helen Christomanou +3 more
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A New Glucosylceramidase Activator in Human Placenta
1986Natural substrates of many lysosomal hydrolases are highly hydrophobic. While the reactions can proceed in vitro when appropriate detergents are included in the assay mixture, these enzymes must function in vivo without artificial detergents of high concentrations often required for in vitro reactions.
Anna Maria Vaccaro +5 more
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International Journal of Peptide Research and Therapeutics, 2008
The mutations in human glucosylceramidase lead to Gaucher disease, which is the most prevalent lysosomal storage disease. So far 153 point mutations have been recorded in human glucosylceramidase, resulting in a wide variability in clinical presentations.
Shaomin Yan, Guang Wu
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The mutations in human glucosylceramidase lead to Gaucher disease, which is the most prevalent lysosomal storage disease. So far 153 point mutations have been recorded in human glucosylceramidase, resulting in a wide variability in clinical presentations.
Shaomin Yan, Guang Wu
openaire +1 more source