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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Autores principales: Lopes, C.H.G.L., Mazzini, M.N., Tortorella, H., Konrath, R.A., Brandelli, A.
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_02820080_v15_n5_p477_Lopes
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spelling 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
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