Results 161 to 170 of about 2,570 (187)
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Reconstitution of glucosylceramidase on binding to acidic phospholipid-containing vesicles
BBA - Proteins and Proteomics, 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
Anna Maria Vaccaro +2 more
exaly +3 more sources
Studies on glucosylceramidase binding to phosphatidylserine liposomes: the role of bilayer curvature
Biochimica Et Biophysica Acta - Biomembranes, 1993The 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 ...
Anna Maria Vaccaro +2 more
exaly +3 more sources
A New Glucosylceramidase Activator in Human Placenta
, 1986 Natural 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
openaire +2 more sources
FEBS Journal, 1985
Properties of glucosylsphingosine (gluco‐psychosine) glucosyl hydrolase were studied in detail in cultured human fibroblasts and placenta and were compared with those of glucosylceramidase. The two activities, that are deficient in tissues of Gaucher patients, showed minor but consistent differences. The pH optima were 4.8 for psychosine hydrolysis and
Anna Maria Vaccaro, Kunihiko Suzuki
exaly +3 more sources
Properties of glucosylsphingosine (gluco‐psychosine) glucosyl hydrolase were studied in detail in cultured human fibroblasts and placenta and were compared with those of glucosylceramidase. The two activities, that are deficient in tissues of Gaucher patients, showed minor but consistent differences. The pH optima were 4.8 for psychosine hydrolysis and
Anna Maria Vaccaro, Kunihiko Suzuki
exaly +3 more sources
Intracellular Activity of Lysosomal Glucosylceramidase Measured with 4-Nonylumbelliferyl β-glucoside
Biological Chemistry Hoppe-Seyler, 1989Enzymatic 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, Gunter Legler
exaly +3 more sources
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, Wu Guang
exaly +2 more sources
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, Wu Guang
exaly +2 more sources
Clinical Biochemistry, 1987
A new protein activator of glucosylceramidase has recently been found in human placenta. In the present work, it has been compared with a previously reported glucosylceramidase activator, the Gaucher factor. The two activators showed different properties.
Anna Maria Vaccaro +2 more
exaly +3 more sources
A new protein activator of glucosylceramidase has recently been found in human placenta. In the present work, it has been compared with a previously reported glucosylceramidase activator, the Gaucher factor. The two activators showed different properties.
Anna Maria Vaccaro +2 more
exaly +3 more sources
Biochimica Et Biophysica Acta - General Subjects, 1990
Optimal enzymatic hydrolysis of glucosylceramide inserted into liposomes has been obtained when both acidic phospholipids and the appropriate fatty acids were added to glucosylceramide-containing liposomes. In fact, the stimulation of glucosylceramidase by acidic phospholipids was synergistically enhanced by fatty acids, whose effect was dependent upon
Anna Maria Vaccaro +2 more
exaly +3 more sources
Optimal enzymatic hydrolysis of glucosylceramide inserted into liposomes has been obtained when both acidic phospholipids and the appropriate fatty acids were added to glucosylceramide-containing liposomes. In fact, the stimulation of glucosylceramidase by acidic phospholipids was synergistically enhanced by fatty acids, whose effect was dependent upon
Anna Maria Vaccaro +2 more
exaly +3 more sources