The trans-sialidase of Trypanosoma cruzi is anchored by two different lipids

The trans-sialidase from the trypomastigote stage of Trypanosoma cruzi was metabolically labeled with [3H]-palmitic acid and purified by immunoprecipitation with a monoclonal antibody. The action of PI-PLC on the immunoprecipitate released a lipid that was analyzed by TLC. Lyso-1-O-h exadecylglycero...

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Autores principales: Agusti, R., Couto, A.S., Campetella, O.E., Frasch, A.C.C., De Lederkremer, R.M.
Formato: JOUR
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GPI
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_09596658_v7_n6_p731_Agusti
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spelling todo:paper_09596658_v7_n6_p731_Agusti2023-10-03T15:53:09Z The trans-sialidase of Trypanosoma cruzi is anchored by two different lipids Agusti, R. Couto, A.S. Campetella, O.E. Frasch, A.C.C. De Lederkremer, R.M. GPI Trans-sialidase Trypanosoma cruzi lipid palmitic acid sialidase article immunoprecipitation nonhuman priority journal thin layer chromatography trypanosoma cruzi Animals Chromatography, Thin Layer Glycosylphosphatidylinositols Membrane Lipids Mice Neuraminidase Phosphatidylinositol Diacylglycerol-Lyase Phospholipase C Substrate Specificity Trypanosoma cruzi Trypanosoma Trypanosoma cruzi The trans-sialidase from the trypomastigote stage of Trypanosoma cruzi was metabolically labeled with [3H]-palmitic acid and purified by immunoprecipitation with a monoclonal antibody. The action of PI-PLC on the immunoprecipitate released a lipid that was analyzed by TLC. Lyso-1-O-h exadecylglycerol and N-palmitoyl-sphinganine were obtained in a 1:3 ratio. A comparison with the GPI anchors present in the different stages of T. ruzi was made. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_09596658_v7_n6_p731_Agusti
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic GPI
Trans-sialidase
Trypanosoma cruzi
lipid
palmitic acid
sialidase
article
immunoprecipitation
nonhuman
priority journal
thin layer chromatography
trypanosoma cruzi
Animals
Chromatography, Thin Layer
Glycosylphosphatidylinositols
Membrane Lipids
Mice
Neuraminidase
Phosphatidylinositol Diacylglycerol-Lyase
Phospholipase C
Substrate Specificity
Trypanosoma cruzi
Trypanosoma
Trypanosoma cruzi
spellingShingle GPI
Trans-sialidase
Trypanosoma cruzi
lipid
palmitic acid
sialidase
article
immunoprecipitation
nonhuman
priority journal
thin layer chromatography
trypanosoma cruzi
Animals
Chromatography, Thin Layer
Glycosylphosphatidylinositols
Membrane Lipids
Mice
Neuraminidase
Phosphatidylinositol Diacylglycerol-Lyase
Phospholipase C
Substrate Specificity
Trypanosoma cruzi
Trypanosoma
Trypanosoma cruzi
Agusti, R.
Couto, A.S.
Campetella, O.E.
Frasch, A.C.C.
De Lederkremer, R.M.
The trans-sialidase of Trypanosoma cruzi is anchored by two different lipids
topic_facet GPI
Trans-sialidase
Trypanosoma cruzi
lipid
palmitic acid
sialidase
article
immunoprecipitation
nonhuman
priority journal
thin layer chromatography
trypanosoma cruzi
Animals
Chromatography, Thin Layer
Glycosylphosphatidylinositols
Membrane Lipids
Mice
Neuraminidase
Phosphatidylinositol Diacylglycerol-Lyase
Phospholipase C
Substrate Specificity
Trypanosoma cruzi
Trypanosoma
Trypanosoma cruzi
description The trans-sialidase from the trypomastigote stage of Trypanosoma cruzi was metabolically labeled with [3H]-palmitic acid and purified by immunoprecipitation with a monoclonal antibody. The action of PI-PLC on the immunoprecipitate released a lipid that was analyzed by TLC. Lyso-1-O-h exadecylglycerol and N-palmitoyl-sphinganine were obtained in a 1:3 ratio. A comparison with the GPI anchors present in the different stages of T. ruzi was made.
format JOUR
author Agusti, R.
Couto, A.S.
Campetella, O.E.
Frasch, A.C.C.
De Lederkremer, R.M.
author_facet Agusti, R.
Couto, A.S.
Campetella, O.E.
Frasch, A.C.C.
De Lederkremer, R.M.
author_sort Agusti, R.
title The trans-sialidase of Trypanosoma cruzi is anchored by two different lipids
title_short The trans-sialidase of Trypanosoma cruzi is anchored by two different lipids
title_full The trans-sialidase of Trypanosoma cruzi is anchored by two different lipids
title_fullStr The trans-sialidase of Trypanosoma cruzi is anchored by two different lipids
title_full_unstemmed The trans-sialidase of Trypanosoma cruzi is anchored by two different lipids
title_sort trans-sialidase of trypanosoma cruzi is anchored by two different lipids
url http://hdl.handle.net/20.500.12110/paper_09596658_v7_n6_p731_Agusti
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