Isolation, partial characterization and biological activity of mannosyl glycopeptides from seminal plasma
Affinity chromatography on Concanavalin-A Sepharose, followed by gel filtration and hydrophobic interaction chromatography, permits the isolation of low molecular weight N-glycosidically linked oligomannosidic glycopeptides (MGp) from the autoproteolysis products of human seminal plasma. The monosac...
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todo:paper_02820080_v15_n5_p477_Lopes2023-10-03T15:17:13Z Isolation, partial characterization and biological activity of mannosyl glycopeptides from seminal plasma Lopes, C.H.G.L. Mazzini, M.N. Tortorella, H. Konrath, R.A. Brandelli, A. Carbohydrate Exocytosis Glycoconjugate Human Semen Sperm glycopeptide mannose acrosome affinity chromatography article carbohydrate analysis exocytosis human male normal human priority journal seminal plasma Acrosome Reaction Carbohydrate Conformation Chromatography, Affinity Chromatography, Gas Chromatography, Gel Exocytosis Glycopeptides Humans Male Mannose Oligosaccharides Semen Affinity chromatography on Concanavalin-A Sepharose, followed by gel filtration and hydrophobic interaction chromatography, permits the isolation of low molecular weight N-glycosidically linked oligomannosidic glycopeptides (MGp) from the autoproteolysis products of human seminal plasma. The monosaccharide composition of MGp showed only mannose, N-acetylglucosamine and a small amount of galactose. Structural studies were carried out by methylation analysis and chromium trioxide oxidation, and results were consistent with the structures accepted for high-mannose N-glycans. MGp was capable of inhibiting the sperm acrosomal exocytosis mediated by sperm- surface receptors. These data suggest that MGp act as a 'decapacitation' factor preventing premature sperm exocytosis. Fil:Mazzini, M.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Tortorella, H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Brandelli, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_02820080_v15_n5_p477_Lopes |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Carbohydrate Exocytosis Glycoconjugate Human Semen Sperm glycopeptide mannose acrosome affinity chromatography article carbohydrate analysis exocytosis human male normal human priority journal seminal plasma Acrosome Reaction Carbohydrate Conformation Chromatography, Affinity Chromatography, Gas Chromatography, Gel Exocytosis Glycopeptides Humans Male Mannose Oligosaccharides Semen |
spellingShingle |
Carbohydrate Exocytosis Glycoconjugate Human Semen Sperm glycopeptide mannose acrosome affinity chromatography article carbohydrate analysis exocytosis human male normal human priority journal seminal plasma Acrosome Reaction Carbohydrate Conformation Chromatography, Affinity Chromatography, Gas Chromatography, Gel Exocytosis Glycopeptides Humans Male Mannose Oligosaccharides Semen Lopes, C.H.G.L. Mazzini, M.N. Tortorella, H. Konrath, R.A. Brandelli, A. Isolation, partial characterization and biological activity of mannosyl glycopeptides from seminal plasma |
topic_facet |
Carbohydrate Exocytosis Glycoconjugate Human Semen Sperm glycopeptide mannose acrosome affinity chromatography article carbohydrate analysis exocytosis human male normal human priority journal seminal plasma Acrosome Reaction Carbohydrate Conformation Chromatography, Affinity Chromatography, Gas Chromatography, Gel Exocytosis Glycopeptides Humans Male Mannose Oligosaccharides Semen |
description |
Affinity chromatography on Concanavalin-A Sepharose, followed by gel filtration and hydrophobic interaction chromatography, permits the isolation of low molecular weight N-glycosidically linked oligomannosidic glycopeptides (MGp) from the autoproteolysis products of human seminal plasma. The monosaccharide composition of MGp showed only mannose, N-acetylglucosamine and a small amount of galactose. Structural studies were carried out by methylation analysis and chromium trioxide oxidation, and results were consistent with the structures accepted for high-mannose N-glycans. MGp was capable of inhibiting the sperm acrosomal exocytosis mediated by sperm- surface receptors. These data suggest that MGp act as a 'decapacitation' factor preventing premature sperm exocytosis. |
format |
JOUR |
author |
Lopes, C.H.G.L. Mazzini, M.N. Tortorella, H. Konrath, R.A. Brandelli, A. |
author_facet |
Lopes, C.H.G.L. Mazzini, M.N. Tortorella, H. Konrath, R.A. Brandelli, A. |
author_sort |
Lopes, C.H.G.L. |
title |
Isolation, partial characterization and biological activity of mannosyl glycopeptides from seminal plasma |
title_short |
Isolation, partial characterization and biological activity of mannosyl glycopeptides from seminal plasma |
title_full |
Isolation, partial characterization and biological activity of mannosyl glycopeptides from seminal plasma |
title_fullStr |
Isolation, partial characterization and biological activity of mannosyl glycopeptides from seminal plasma |
title_full_unstemmed |
Isolation, partial characterization and biological activity of mannosyl glycopeptides from seminal plasma |
title_sort |
isolation, partial characterization and biological activity of mannosyl glycopeptides from seminal plasma |
url |
http://hdl.handle.net/20.500.12110/paper_02820080_v15_n5_p477_Lopes |
work_keys_str_mv |
AT lopeschgl isolationpartialcharacterizationandbiologicalactivityofmannosylglycopeptidesfromseminalplasma AT mazzinimn isolationpartialcharacterizationandbiologicalactivityofmannosylglycopeptidesfromseminalplasma AT tortorellah isolationpartialcharacterizationandbiologicalactivityofmannosylglycopeptidesfromseminalplasma AT konrathra isolationpartialcharacterizationandbiologicalactivityofmannosylglycopeptidesfromseminalplasma AT brandellia isolationpartialcharacterizationandbiologicalactivityofmannosylglycopeptidesfromseminalplasma |
_version_ |
1807319922681839616 |