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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Detalles Bibliográficos
Autores principales: GROISMAN, J.F., de LEDERKREMER, R.M.
Formato: JOUR
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: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 todo:paper_00142956_v165_n2_p327_GROISMAN
record_format dspace
spelling todo:paper_00142956_v165_n2_p327_GROISMAN2023-10-03T14:11:50Z d‐Galactofuranose in the N‐linked sugar chain of a glycopeptide from Ascobolus furfuraceus GROISMAN, J.F. de LEDERKREMER, R.M. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, J.F.
de LEDERKREMER, R.M.
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
format JOUR
author GROISMAN, J.F.
de LEDERKREMER, R.M.
author_facet GROISMAN, J.F.
de LEDERKREMER, R.M.
author_sort GROISMAN, J.F.
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
url http://hdl.handle.net/20.500.12110/paper_00142956_v165_n2_p327_GROISMAN
work_keys_str_mv AT groismanjf dgalactofuranoseinthenlinkedsugarchainofaglycopeptidefromascobolusfurfuraceus
AT delederkremerrm dgalactofuranoseinthenlinkedsugarchainofaglycopeptidefromascobolusfurfuraceus
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