Results 181 to 190 of about 3,748 (212)

Studies on glucosylceramidase binding to phosphatidylserine liposomes: the role of bilayer curvature

Biochimica Et Biophysica Acta - 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 ...
Anna Maria Vaccaro, Massimo Tatti, Fiorella Ciaffoni   +2 more
exaly   +4 more sources

Current and Novel Aspects on the Non-lysosomal β-Glucosylceramidase GBA2

Neurochemical Research, 2015
The non-lysosomal β-glucosylceramidase GBA2 (EC3.2.1.45, GH116) is ubiquitously expressed in various mammal tissues and cell types where it catalyzes the hydrolysis of glucosylceramide into glucose and ceramide. Although it has been known for many years that the central nervous system is the main site of GBA2 expression and activity, little information
Massimo Aureli, Maura Samarani, Nicoletta Loberto, Giulia Mancini, Valentina Murdica, Elena Chiricozzi, Alessandro Prinetti, Bassi Rosaria, Sonnino Sandro   +8 more
exaly   +5 more sources

Correlation between the activity of glucosylceramidase and its binding to glucosylceramide-containing liposomes. Role of acidic phospholipids and fatty acids

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, Massimo Tatti, Rosa Salvioli   +2 more
exaly   +4 more sources

Effect of a heat-stable factor in human placenta on glucosylceramidase, glucosylsphingosine glucosyl hydrolase, and acid β-glucosidase activities

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, Massimo Tatti, Rosa Salvioli   +2 more
exaly   +4 more sources

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Reconstitution of glucosylceramidase on binding to acidic phospholipid-containing vesicles

BBA - Proteins and Proteomics, 1992
Studies 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, Massimo Tatti, Fiorella Ciaffoni   +2 more
exaly   +3 more sources

Glucosylceramidase Activator Deficiency

, 2009
David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen‐Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, Alexander K. C. Leung, William Lane M. Robson, Andrew L. Wong, Manisha Balwani, Ainu Prakash‐Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Läng, Hugo Ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Dêbiec, Christian Hugo, Brigitte M. Lobnig, Brigitte M. Lobnig, John‐John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. De Vivo, Stefan Kölker, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs‐Raine, Seda Sancak, Ralf Paschke, Dorin‐Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler‐Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier‐Zepter, Klaus Rüether   +99 more
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Purification of glucosylceramidase by affinity chromatography

Canadian Journal of Biochemistry, 1982
Glucosylceramide:β-glucosidase (glucocerebrosidase, EC 3.2.1.45) has been purified 12 900-fold from human placenta using a specific affinity column. The ligand, glucosyl sphingosine, prepared from glucocerebroside by alkaline hydrolysis, was attached to epoxy-activated Sepharose 6B.
P M, Strasberg, J A, Lowden, D, Mahuran
openaire   +2 more sources

Glucosylceramidase degradation in fibroblasts carrying bi-allelic Parkin mutations

Molecular Genetics and Metabolism, 2013
Alisdair McNeill, Daniel G Healy, Anthony H V Schapira   +2 more
exaly   +3 more sources

Accumulation of Tissue Glucosylsphingosine in Gaucher-like Mouse Induced by the Glucosylceramidase Inhibitor Cyclophellitol

Archives of Biochemistry and Biophysics, 1993
Shinichiro Atsumi, Chisato Nosaka, H. Iinuma, Kazuo Umezawa   +3 more
openalex   +3 more sources

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, Gunter Legler
exaly   +3 more sources