Biosynthesis of guinea pig erythrocyte triglycosylceramide by bone marrow beta-N-acetylgalactosaminyltransferase
| Autor: | Manju Basu, Subhash Basu, Jao-Long Chien |
|---|---|
| Rok vydání: | 1974 |
| Předmět: |
Sucrose
Erythrocytes Guinea Pigs Biophysics Galactosamine Lactose Biology Biochemistry Guinea pig chemistry.chemical_compound Lactosylceramide Biosynthesis Cerebrosides Bone Marrow Gangliosides medicine Animals Centrifugation Carbon Radioisotopes music Molecular Biology chemistry.chemical_classification Manganese music.instrument Cell Biology Uridine Diphosphate Sugars Kinetics Enzyme medicine.anatomical_structure Hexosaminidases chemistry Hexosyltransferases Autoradiography Bone marrow Chromatography Thin Layer Glycolipids Homogenization (biology) |
| Zdroj: | Biochemical and biophysical research communications. 60(3) |
| ISSN: | 0006-291X |
| Popis: | A β-N-acetylgalactosaminyltransferases (Ga1NAcT) that catalyzes the synthesis of a triglycosylceramide, GanglioTricer (Ga1NAcβ-Ga1β1-4G1c-cer), from lactosylceramide and UDP-Ga1NAc was isolated from guinea pig bone marrow. The enzyme was present in the supernatant solution obtained after homogenization of guinea pig bone marrow 12,000 × g pellet with 0.32 M sucrose containing 0.6% Triton X-100 and centrifugation at 129,000 × g. The enzyme that catalyzed the transfer of Ga1NAc to a tetraglycosylceramide (Lac-nTet-cer) was found in a membrane-bound fraction. The K m values were 0.5 mM and 0.7 mM for the lactosylceramide and Lac-nTet-cer, respectively. 97.0% of the terminal [ 14 C]Ga1NAc was cleaved by the action of pure β-hexosaminidase from [ 14 C]triglycosylceramide. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|