Distribution in spleen subcellular organelles of sialidase active towards natural sialoglycolipid and sialoglycoprotein substrates
| Autor: | Joseph T. Nelson, Cara Lynne Schengrund, Mary Ann Repman |
|---|---|
| Rok vydání: | 1979 |
| Předmět: |
Ganglioside
biology Sialoglycoproteins Succinate dehydrogenase Neuraminidase Substrate (chemistry) General Medicine Sialidase Substrate Specificity Sialic acid Membrane Lipids chemistry.chemical_compound Biochemistry chemistry Sialoglycoprotein Gangliosides Organelle biology.protein Animals Humans Cattle Spleen Subcellular Fractions |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Enzymology. 568:377-385 |
| ISSN: | 0005-2744 |
| Popis: | A procedure was devised for the preparation of enriched populations of subcellular organelles from homogenized bovine spleen. The fractions obtained were characterized for arysulfatase, succinate dehydrogenase, UDPgalactosyltransferase and 5′-nucleotidase activities. The distribution of sialidase (acylneuraminyl hydrolase, EC 3.2.1.18) activity directed towards either endogenous substrate or exogenous ganglioside substrate suggests that it is enriched in the plasma membrane/microsomal fractions. Sialidase activity towards exogenous sialoglycoproteins, isolated from erythrocyte membranes, was enriched in the least dense of the plasma membrane/microsomal-containing fractions. The endogenous sialidase substrates were primarily the sialoglycolipids, hematoside and disialogangliosides. At the pH optimum, 3.8 and 37°C, release of endogeneous sialic acid was linear with time for 3 h. At the end of this time, 85% or more of the available endogenous substrate was hydrolyzed. |
| Databáze: | OpenAIRE |
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