d‐Galactofuranose in the N‐linked sugar chain of a glycopeptide from Ascobolus furfuraceus

Two types of linkages between the carbohydrate and the peptide moiety in the glycopeptide from Ascobolus furfuraceus are described. Treatment with mild alkali produced β‐elimination of a small oligosaccharide. Evidence for the O‐glycosidic linkage was provided by (a) increase in absorbance at 240 nm...

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Autores principales:	Groisman, José Felipe, Muchnik de Lederkremer, Rosa María
Publicado:	1987
Materias:	acetylglucosaminidase amino acid galactose glycopeptide Mannosyl Glycoprotein Endo beta N Acetylglucosaminidase n acetyl beta glucosaminidase article Ascomycetes gel chromatography methylation nuclear magnetic resonance spectroscopy optical rotation oxidation reduction reaction paper chromatography pH Acetylglucosaminidase Amino Acids Ascomycota Chromatography, Gel Chromatography, Paper Galactose Glycopeptides Hydrogen-Ion Concentration Magnetic Resonance Spectroscopy Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase Methylation Optical Rotation Oxidation-Reduction Support, Non-U.S. Gov't
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v165_n2_p327_GROISMAN http://hdl.handle.net/20.500.12110/paper_00142956_v165_n2_p327_GROISMAN
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00142956_v165_n2_p327_GROISMAN
record_format	dspace
spelling	paper:paper_00142956_v165_n2_p327_GROISMAN2023-06-08T14:36:39Z d‐Galactofuranose in the N‐linked sugar chain of a glycopeptide from Ascobolus furfuraceus Groisman, José Felipe Muchnik de Lederkremer, Rosa María acetylglucosaminidase amino acid galactose glycopeptide Mannosyl Glycoprotein Endo beta N Acetylglucosaminidase n acetyl beta glucosaminidase article Ascomycetes gel chromatography methylation nuclear magnetic resonance spectroscopy optical rotation oxidation reduction reaction paper chromatography pH Acetylglucosaminidase Amino Acids Ascomycota Chromatography, Gel Chromatography, Paper Galactose Glycopeptides Hydrogen-Ion Concentration Magnetic Resonance Spectroscopy Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase Methylation Optical Rotation Oxidation-Reduction Support, Non-U.S. Gov't Two types of linkages between the carbohydrate and the peptide moiety in the glycopeptide from Ascobolus furfuraceus are described. Treatment with mild alkali produced β‐elimination of a small oligosaccharide. Evidence for the O‐glycosidic linkage was provided by (a) increase in absorbance at 240 nm, (b) decrease in threonine and serine content after the alkaline treatment and (c) detection of tritiated oligosaccharide following alkaline NaB3H4 reduction. Mannose is the sugar involved in the O‐glycosidic linkage. The remaining glycopeptide was branched by galactofuranose units, which were selectivity released by mild acid hydrolysis. The N‐glycosidic linkage of the sugar chain was conclusively proved by cleavage with endo‐β‐N‐acetyl‐glucosaminidase. Sequential NaB3H4 reduction and acid hydrolysis gave [3H]glucosaminitol. The structure of the sugar chain was studied by 13C NMR spectroscopy and by methylation analysis. Copyright © 1987, Wiley Blackwell. All rights reserved Fil:GROISMAN, J.F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 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_00142956_v165_n2_p327_GROISMAN http://hdl.handle.net/20.500.12110/paper_00142956_v165_n2_p327_GROISMAN
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	acetylglucosaminidase amino acid galactose glycopeptide Mannosyl Glycoprotein Endo beta N Acetylglucosaminidase n acetyl beta glucosaminidase article Ascomycetes gel chromatography methylation nuclear magnetic resonance spectroscopy optical rotation oxidation reduction reaction paper chromatography pH Acetylglucosaminidase Amino Acids Ascomycota Chromatography, Gel Chromatography, Paper Galactose Glycopeptides Hydrogen-Ion Concentration Magnetic Resonance Spectroscopy Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase Methylation Optical Rotation Oxidation-Reduction Support, Non-U.S. Gov't
spellingShingle	acetylglucosaminidase amino acid galactose glycopeptide Mannosyl Glycoprotein Endo beta N Acetylglucosaminidase n acetyl beta glucosaminidase article Ascomycetes gel chromatography methylation nuclear magnetic resonance spectroscopy optical rotation oxidation reduction reaction paper chromatography pH Acetylglucosaminidase Amino Acids Ascomycota Chromatography, Gel Chromatography, Paper Galactose Glycopeptides Hydrogen-Ion Concentration Magnetic Resonance Spectroscopy Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase Methylation Optical Rotation Oxidation-Reduction Support, Non-U.S. Gov't Groisman, José Felipe Muchnik de Lederkremer, Rosa María d‐Galactofuranose in the N‐linked sugar chain of a glycopeptide from Ascobolus furfuraceus
topic_facet	acetylglucosaminidase amino acid galactose glycopeptide Mannosyl Glycoprotein Endo beta N Acetylglucosaminidase n acetyl beta glucosaminidase article Ascomycetes gel chromatography methylation nuclear magnetic resonance spectroscopy optical rotation oxidation reduction reaction paper chromatography pH Acetylglucosaminidase Amino Acids Ascomycota Chromatography, Gel Chromatography, Paper Galactose Glycopeptides Hydrogen-Ion Concentration Magnetic Resonance Spectroscopy Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase Methylation Optical Rotation Oxidation-Reduction Support, Non-U.S. Gov't
description	Two types of linkages between the carbohydrate and the peptide moiety in the glycopeptide from Ascobolus furfuraceus are described. Treatment with mild alkali produced β‐elimination of a small oligosaccharide. Evidence for the O‐glycosidic linkage was provided by (a) increase in absorbance at 240 nm, (b) decrease in threonine and serine content after the alkaline treatment and (c) detection of tritiated oligosaccharide following alkaline NaB3H4 reduction. Mannose is the sugar involved in the O‐glycosidic linkage. The remaining glycopeptide was branched by galactofuranose units, which were selectivity released by mild acid hydrolysis. The N‐glycosidic linkage of the sugar chain was conclusively proved by cleavage with endo‐β‐N‐acetyl‐glucosaminidase. Sequential NaB3H4 reduction and acid hydrolysis gave [3H]glucosaminitol. The structure of the sugar chain was studied by 13C NMR spectroscopy and by methylation analysis. Copyright © 1987, Wiley Blackwell. All rights reserved
author	Groisman, José Felipe Muchnik de Lederkremer, Rosa María
author_facet	Groisman, José Felipe Muchnik de Lederkremer, Rosa María
author_sort	Groisman, José Felipe
title	d‐Galactofuranose in the N‐linked sugar chain of a glycopeptide from Ascobolus furfuraceus
title_short	d‐Galactofuranose in the N‐linked sugar chain of a glycopeptide from Ascobolus furfuraceus
title_full	d‐Galactofuranose in the N‐linked sugar chain of a glycopeptide from Ascobolus furfuraceus
title_fullStr	d‐Galactofuranose in the N‐linked sugar chain of a glycopeptide from Ascobolus furfuraceus
title_full_unstemmed	d‐Galactofuranose in the N‐linked sugar chain of a glycopeptide from Ascobolus furfuraceus
title_sort	d‐galactofuranose in the n‐linked sugar chain of a glycopeptide from ascobolus furfuraceus
publishDate	1987
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v165_n2_p327_GROISMAN http://hdl.handle.net/20.500.12110/paper_00142956_v165_n2_p327_GROISMAN
work_keys_str_mv	AT groismanjosefelipe dgalactofuranoseinthenlinkedsugarchainofaglycopeptidefromascobolusfurfuraceus AT muchnikdelederkremerrosamaria dgalactofuranoseinthenlinkedsugarchainofaglycopeptidefromascobolusfurfuraceus
_version_	1768544985096912896

d‐Galactofuranose in the N‐linked sugar chain of a glycopeptide from Ascobolus furfuraceus

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