Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi
Labeled sialoglycolipids were purified from tissue culture-derived trypomastigotes incubated with [3H]fetuin. Thin layer chromatography of [3H]sialoglycolipids showed three components with the same migration as gangliosides extracted from parasites incubated with [3H]palmitic acid. Neuraminidase tre...
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1987
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01666851_v26_n1-2_p135_Zingales http://hdl.handle.net/20.500.12110/paper_01666851_v26_n1-2_p135_Zingales |
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paper:paper_01666851_v26_n1-2_p135_Zingales2023-06-08T15:16:03Z Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi Muchnik de Lederkremer, Rosa María Sialic acid Sialic acid transglycosylase Sialidase Sialoglycolipid Sialyl transferase Trypanosoma cruzi alpha fetoprotein beta D galactoside alpha 2 6 sialyltransferase beta-D-galactoside alpha 2-6-sialyltransferase glycoconjugate glycolipid sialic acid derivative sialoglycolipids sialyltransferase animal article enzymology metabolism paper chromatography thin layer chromatography Trypanosoma cruzi alpha-Fetoproteins Animal Chromatography, Paper Chromatography, Thin Layer Glycoconjugates Glycolipids Sialic Acids Sialyltransferases Support, Non-U.S. Gov't Trypanosoma cruzi Labeled sialoglycolipids were purified from tissue culture-derived trypomastigotes incubated with [3H]fetuin. Thin layer chromatography of [3H]sialoglycolipids showed three components with the same migration as gangliosides extracted from parasites incubated with [3H]palmitic acid. Neuraminidase treatment or mild acid hydrolysis confirmed the presence of [3H]sialyl residues in sialoglycolipids synthesized after [3H]fetuin incubation. Labeling was not observed when parasites were incubated with free [3H]sialic acid (C7 derivative), suggesting that sialyl residues are directly transferred in vivo to gangliosides, by an enzymatic reaction possibly catalysed by a sialyl transferase (transglycosylase). Sonicated extracts of trypomastigotes incubated with [3H]fetuin catalysed the labeling of endogenous glycoconjugates as well as of bovine brain gangliosides. The transglycosylase activity was found associated with the particulate fraction and could be solubilized with Triton X-100. The specific activity of the sialic acid transglycosylase in epimastigotes is 17% of that found in trypomastigotes. Addition of an excess free sialic acid did not inhibit the reaction, suggesting that transfer does not occur via a pool of free sialic acid. © 1987. Fil:de Lederkremer, R.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1987 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01666851_v26_n1-2_p135_Zingales http://hdl.handle.net/20.500.12110/paper_01666851_v26_n1-2_p135_Zingales |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Sialic acid Sialic acid transglycosylase Sialidase Sialoglycolipid Sialyl transferase Trypanosoma cruzi alpha fetoprotein beta D galactoside alpha 2 6 sialyltransferase beta-D-galactoside alpha 2-6-sialyltransferase glycoconjugate glycolipid sialic acid derivative sialoglycolipids sialyltransferase animal article enzymology metabolism paper chromatography thin layer chromatography Trypanosoma cruzi alpha-Fetoproteins Animal Chromatography, Paper Chromatography, Thin Layer Glycoconjugates Glycolipids Sialic Acids Sialyltransferases Support, Non-U.S. Gov't Trypanosoma cruzi |
| spellingShingle |
Sialic acid Sialic acid transglycosylase Sialidase Sialoglycolipid Sialyl transferase Trypanosoma cruzi alpha fetoprotein beta D galactoside alpha 2 6 sialyltransferase beta-D-galactoside alpha 2-6-sialyltransferase glycoconjugate glycolipid sialic acid derivative sialoglycolipids sialyltransferase animal article enzymology metabolism paper chromatography thin layer chromatography Trypanosoma cruzi alpha-Fetoproteins Animal Chromatography, Paper Chromatography, Thin Layer Glycoconjugates Glycolipids Sialic Acids Sialyltransferases Support, Non-U.S. Gov't Trypanosoma cruzi Muchnik de Lederkremer, Rosa María Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi |
| topic_facet |
Sialic acid Sialic acid transglycosylase Sialidase Sialoglycolipid Sialyl transferase Trypanosoma cruzi alpha fetoprotein beta D galactoside alpha 2 6 sialyltransferase beta-D-galactoside alpha 2-6-sialyltransferase glycoconjugate glycolipid sialic acid derivative sialoglycolipids sialyltransferase animal article enzymology metabolism paper chromatography thin layer chromatography Trypanosoma cruzi alpha-Fetoproteins Animal Chromatography, Paper Chromatography, Thin Layer Glycoconjugates Glycolipids Sialic Acids Sialyltransferases Support, Non-U.S. Gov't Trypanosoma cruzi |
| description |
Labeled sialoglycolipids were purified from tissue culture-derived trypomastigotes incubated with [3H]fetuin. Thin layer chromatography of [3H]sialoglycolipids showed three components with the same migration as gangliosides extracted from parasites incubated with [3H]palmitic acid. Neuraminidase treatment or mild acid hydrolysis confirmed the presence of [3H]sialyl residues in sialoglycolipids synthesized after [3H]fetuin incubation. Labeling was not observed when parasites were incubated with free [3H]sialic acid (C7 derivative), suggesting that sialyl residues are directly transferred in vivo to gangliosides, by an enzymatic reaction possibly catalysed by a sialyl transferase (transglycosylase). Sonicated extracts of trypomastigotes incubated with [3H]fetuin catalysed the labeling of endogenous glycoconjugates as well as of bovine brain gangliosides. The transglycosylase activity was found associated with the particulate fraction and could be solubilized with Triton X-100. The specific activity of the sialic acid transglycosylase in epimastigotes is 17% of that found in trypomastigotes. Addition of an excess free sialic acid did not inhibit the reaction, suggesting that transfer does not occur via a pool of free sialic acid. © 1987. |
| author |
Muchnik de Lederkremer, Rosa María |
| author_facet |
Muchnik de Lederkremer, Rosa María |
| author_sort |
Muchnik de Lederkremer, Rosa María |
| title |
Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi |
| title_short |
Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi |
| title_full |
Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi |
| title_fullStr |
Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi |
| title_full_unstemmed |
Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi |
| title_sort |
direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of trypanosoma cruzi |
| publishDate |
1987 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01666851_v26_n1-2_p135_Zingales http://hdl.handle.net/20.500.12110/paper_01666851_v26_n1-2_p135_Zingales |
| work_keys_str_mv |
AT muchnikdelederkremerrosamaria directsialicacidtransferfromaproteindonortoglycolipidsoftrypomastigoteformsoftrypanosomacruzi |
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1768541886574755840 |