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Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85,SB_86

• Article ID: 2451
  Lis H, Sharon N "Protein glycosylation. Structural and functional aspects" - European Journal of Biochemistry 218 (1993) 1-27
  

  During the last decade, there have been enormous advances in our knowledge of glycoproteins and the stage has been set for the biotechnological production of many of them for therapeutic use. These advances are reviewed, with special emphasis on the structure and function of the glycoproteins (excluding the proteoglycans). Current methods for structural analysis of glycoproteins are surveyed, as are novel carbohydrate-peptide linking groups, and mono- and oligo-saccharide constituents found in these macromolecules. The possible roles of the carbohydrate units in modulating the physicochemical and biological properties of the parent proteins are discussed, and evidence is presented on their roles as recognition determinants between molecules and cells, or cell and cells. Finally, examples are given of changes that occur in the carbohydrates of soluble and cell-surface glycoproteins during differentiation, growth and malignancy, which further highlight the important role of these substances in health and disease.

  NCBI PubMed ID: 8243456
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Institutions: Department of Membrane Research and Biophysics, Weizmann Institute of Science, Rehovot, Israel
  
   
  
  Erythrina corallodendron
  CSDB ID 124349 (all data & tools)
• Article ID: 10007
  Kimura Y, Hase S, Ikenaka T, Funatsu G "Structural analyses of sugar chains from Abrus precatorius agglutinin" - Biochimica et Biophysica Acta 966 (1988) 160-167
  

  The structures of asparagine-linked sugar chains of Abrus precatorius agglutinin were determined. The sugar chains were liberated from the lectin by hydrazinolysis. After N-acetylation, the reducing-end residues of the sugar chains were coupled with 2-aminopyridine. The pyridylamino (PA-) derivatives thus obtained were purified by gel filtration and HPLC. The structures of the purified derivatives were identified by component analysis, comparison of their elution positions on HPLC with those of PA-sugar chains of known structures, stepwise exoglycosidase digestion, and partial acetolysis. The major four surgar chains obtained from A. precatorius agglutinin were Manα1→2Manα1→6(Manα1→3)Manβ1→6(Manα1→2Manα2→2Manα1→3)Manα1→GlcNAcβ1→GlcNAc-PA, Manα1→2Manα1→6(Manα1→3)Manα1→6(Manα1→2Manα1→3)Manβ1→GlcNAcβ1→GlcNAc-PA, Manα1→6(Manα1→3)Manα1→6(Manα1→2Manα1→3)Manβ1→4GlcNAcβ1→4GlcNAc-PA, and Manα1→6(Manα1→34) (Xylβ1→2)Manβ1→4GlcNAcβ1→4(Fucα1→3)GlcNAc-PA.

  lectin, glycoprotein, Agglutinin, Sugar chain structure, Pyridylamino derivative, Sugar chain processing, A. precatorius

  Publication DOI: 10.1016/0304-4165(88)90139-0
  Journal NLM ID: 0217513
  Publisher: Elsevier
  Institutions: Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoa, Japan, Department of Chemistry, Osaka University College of Science, Osaka, Japan
  Methods: gel filtration, acid hydrolysis, HPLC, enzymatic digestion, hydrazinolysis, partial acetolysis
  
   
  
  Abrus precatorius
  CSDB ID 109190 (all data & tools)
• Article ID: 10167
  Kimura Y, Suehisa H, Yamaguchi O, Nakajima S, Takagi S "Structures of sugar chains of water-soluble glycoproteins in developing castor bean cotyledons" - Agricultural and Biological Chemistry 54 (1990) 3259-3267
  

  The structures of sugar chains from the water-soluble glycoproteins in developing castor beans have been identified. The structural analyses were done by a fluorescence method combined with exoglycosidase digestions and 1H-NMR spectroscopy. The identified structures fell into two categories; one was an oligomannose-type, the other xylomannose-type or xylose-containing type. Among these oligosaccharides, Man3Fuc1Xyl1GlcNAc2 (M3FX; 38%) and Man6GlcNAc2 (M6B; 22%) were the major structures. The higher mannose-content oligosaccharides (Man8-7GlcNAc2) were only 4.1%, and the further-modified structures (GNM3FX, M2FX) than M3FX were 22% of the total.

  NCBI PubMed ID: 1368642
  Journal NLM ID: 0370452
  WWW link: http://ci.nii.ac.jp/naid/110006324732
  Publisher: Tokyo: Agricultural Chemical Society Of Japan
  Institutions: Department of Agricultural Sciences, Faculty of Agriculture, Okayama University, Japan
  Methods: 1H NMR, HPLC, enzymatic digestion, pyridylamination
  
   
  
  Ricinus communis
  CSDB ID 101375 (all data & tools)
• Article ID: 10190
  Kimura Y, Nakagawa Y, Tokuda T, Yamai M, Nakajima S, Higashide E, Takagi S, Takagi SS "Structures of N-linked oligosaccharides of microsomal glycoproteins from developing castor bean endosperms" - Bioscience, Biotechnology, and Biochemistry 56 (1992) 215-222
  

  The structures of sugar chains of the glycoproteins from the microsomal fraction of developing castor bean endosperms have been analyzed. The structural analyses were done by a fluorescence method combined with component analysis, exoglycosidase digestions, partial acetolysis, Smith degradation, and 1H-NMR spectroscopy. The estimated structures fell into three categories; the first was oligomannose-type, the second xylomannose-type, the third complex-type. Among these oligosaccharides, Man3Fuc1Xyl1GlcNAc2 (M3FX) and Man6GlcNAc2 (M6B) were the major structures. The structures of Man4GlcNAc2 (M4C) and Man4Xyl1GlcNAc2 (M4X) have also been found in the microsomal glycoproteins of the developing bean endosperms. These results could indicate that the structures of M4C, M4X, and M3FX are formed in the stage of sugar chain processing in the microsomal fraction, in which oligomannose-type sugar chains are modified into complex-type ones by several kinds of processing enzymes.

  NCBI PubMed ID: 1368297
  Journal NLM ID: 9205717
  Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
  Institutions: Division of Bio-resource Science, Graduate School of Natural Science and Technology, Okayama University, Japan
  Methods: 1H NMR, Smith degradation, enzymatic digestion, partial acetolysis
  
   
  
  Ricinus communis
  CSDB ID 111159 (all data & tools)
• Article ID: 10243
  Yamaguchi H, Funaoka H, Iwamoto H "Structures of sugar chains of the subunits of an α-amylase inhibitor from Phaseolus vulgaris white kidney beans" - Journal of Biochemistry 111 (1992) 388-395
  

  The structures of asparagine-linked oligosaccharides in the subunits of an α-amylase inhibitor from the white kidney bean (Phaseolus vulgaris) were determined. Glycopeptides obtained from each subunit were treated with hydrazine, then N-acetylated. The oligosaccharides thus liberated were labeled with 2-aminopyridine at their reducing ends and purified by gel-permeation, reverse-phase, and size-fractionation HPLC. The structures of seven oligosaccharides from the α-subunit and eight oligosaccharides from the β-subunit were determined by a combination of composition and molecular size analyses, exo- and endoglycosidase digestions, partial acetolysis, and 1H-NMR spectroscopy. The major glycan chains in the α-subunit were Man α1-6 (Manα1-3) Manα1-6 (Manα1-2Manα1-3)-Manβ1-4GlcNAcβ1-4GlcNAc and (Man α1-2) Manα1-6 (Manα1-2Manα1-3) Manα1-6 (Man-α1-2Manα1-2Manα1-3) Manβ1-4GlcNAcβ1-4GlcNAc, while a glycan chain Manα1-6 (Man-α1-3) (Xy1α1-2) Manβ1-4GlcNAcβ1-4GlcNAc comprised more than 70% of the sugar moiety of the β-subunit.

  NCBI PubMed ID: 1587803
  Journal NLM ID: 0376600
  Publisher: Japanese Biochemical Society
  Institutions: Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture, Japan, Department of Food Science and Technology, Faculty of Engineering, Fukuyama University, Japan
  Methods: 1H NMR, gel filtration, GLC, HPLC, enzymatic digestion, partial acetolysis
  
   
  
  Phaseolus vulgaris
  CSDB ID 132701 (all data & tools)
• Article ID: 10244
  Takahashi N, Hitotsuya H, Hanzawa H, Arata Y, Kurihara Y "Structural study of asparagine-linked oligosaccharide moiety of taste- modifying protein, miraculin" - Journal of Biological Chemistry 265 (1990) 7793-7798
  

  The structures of the N-linked oligosaccharides of miraculin, which is a taste modifying glycoprotein isolated from miracle fruits, berries of Richadella dulcifica, are reported. Asparagine-linked oligosaccharides were released from the protein by glycopeptidase (almond) digestion. The reducing ends of the oligosaccharide chains thus obtained were aminated with a fluorescent reagent, 2-aminopyridine, and the mixture of pyridylamino derivatives of the oligosaccharides was separated by high performance liquid chromatography (HPLC) on an ODS-silica column. More than five kinds of oligosaccharide fractions were separated by the one chromatographic run. The structure of each oligosaccharide thus isolated was analyzed by a combination of sequential exoglycosidase digestion and another kind of HPLC with an amidesilica column. Furthermore, high resolution proton nuclear magnetic resonance (1H NMR) measurements were carried out. It was found that 1) five oligosaccharides obtained are a series of compounds with xylose-containing common structural core, Xyl β1----2 (Man α1----6) Man β1----4-GlcNAc β1----4 (Fuca1----3)GlcNAc, 2) a variety of oligosaccharide structures are significant for two glycosylation sites, Asn-42 and Asn-186, and 3) two new oligosaccharides, B and D, with unusual structures containing monoantennary complex-type were characterized. (formula; see text)

  NCBI PubMed ID: 2335505
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Institutions: Faculty of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan, Department of Biochemistry, Nagoya City University College of Nursing, Japan, Department of Chemistry, Faculty of Education, Yokohama National University, Yokohama, Japan
  Methods: 1H NMR, gel filtration, HPLC, enzymatic digestion
  
   
  
  Richadella dulcifica
  CSDB ID 135862 (all data & tools)
• Article ID: 10246
  Kurosaka A, Yano A, Itoh N, Kuroda Y, Nakagawa T, Kawasaki T "The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum" - Journal of Biological Chemistry 266 (1991) 4168-4172
  

  Antiserum raised against horseradish peroxidase (HRP) recognizes a neural specific carbohydrate antigen in Drosophila and other insects. The epitopic activity of the carbohydrate moiety of HRP recognized by anti-HRP antiserum was measured by a newly developed enzyme-linked immunosorbent assay, in which HRP glycopeptides conjugated with bovine serum albumin were coated onto the wells and then reacted with goat anti-HRP antiserum. HRP sugar moieties released by almond glycopeptidase A digestion of HRP pepsin digests were subjected to pyridylamination. Pyridylamino oligosaccharides were separated into seven fractions by reverse-phase high performance liquid chromatography. The major fraction, which comprised about 80% of the total sugars, reacted strongly with anti-HRP antiserum. The carbohydrate structure of this fraction was determined by sugar composition analysis and 600-MHz 1H NMR spectroscopy as follows: Man α1----6(Man α1----3)(Xyl β1----2)Man β1----4GlcNAc β1----4(Fuc α1----3)GlcNAc. Analyses of reactivity with anti-HRP antiserum of various oligosaccharide derivatives obtained from the major fraction by exoglycosidase digestion and partial acid hydrolysis indicated that α1----6-linked mannose and α1----3-linked fucose are predominantly involved in the epitopic structure.

  NCBI PubMed ID: 1705547
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Institutions: Department of Biotechnology, Faculty of Engineering, Sangyo University, Japan
  
   
  
  Armoracia rusticana
  CSDB ID 136047 (all data & tools)
• Article ID: 10356
  Woodward JR, Craik D, Dell A, Khoo KH, Munro SLA, Clarke AE, Bacic A "Structural analysis of the N-linked glycan chains from a stylar glycoprotein associated with expression of self-incompatibility in Nicotiana alata" - Glycobiology 2 (1992) 241-250
  

  Self-incompatibility in flowering plants of the family Solanaceae is mediated by the product of the S-allele. The allelic products of the S-gene in the female sexual tissues of the pistil are glycoproteins in the mol. wt range 28-32 kDa. These S-glycoproteins have been isolated from styles of Nicotiana alata, homozygous for the S1- and S2-alleles. Earlier studies have indicated that the single potential N-glycosylation site on the S1-glycoprotein bears a glycan chain, whereas of the four potential N-glycosylation sites on the S2-glycoprotein, three are glycosylated. This paper describes the purification and characterization of the N-linked glycan chains from these two glycoproteins. Oligosaccharides were cleaved off the glycoproteins using peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase F (N-glycanase F) and separated by anion-exchange HPLC. Four types of hybrid structure were defined by chemical techniques, fast atom bombardment-mass spectrometry (FAB-MS) and 1H-NMR. Although the relative amounts differed, all four structures were found on both the S1- and S2-glycoproteins, and are heterogeneous at some N-glycosylation sites. No O-linked glycans were detected on the S2-glycoprotein. These results are discussed in relation to the potential of the structural diversity residing in this array of glycoforms to play a rôle in allelic specificity.

  NCBI PubMed ID: 1498421
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Parkville, Australia
  Methods: 1H NMR, gel filtration, FAB-MS, GC-MS, SDS-PAGE, HPLC, enzymatic digestion, methylation analysis, PC
  
   
  
  Brassica campestris
  CSDB ID 126631 (all data & tools)
• Article ID: 10517
  Stahl B, Klabunde T, Witzel H, Krebs B, Steup M, Karas M, Hillenkamp F "The oligosaccharides of the Fe(III)-Zn(II) purple acid phosphatase of the red kidney bean. Determination of the structure by a combination of matrix-assisted laser desorption/ionization mass spectrometry and selective enzymic degradation" - European Journal of Biochemistry 220 (1994) 321-330
  

  Purple acid phosphatase of the common bean Phaseolus vulgaris (KBPase), a dimeric 110-kDa glycoprotein related to the mammalian purple acid phosphatases with a two-metal cluster at the active site contains five oligosaccharide side chains/monomer. The N-linked glycan structures were characterized by selective enzymic degradation in combination with matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). The purified protein was cleaved by cyanogen bromide. One 30-kDa large methionine-free fragment required a further tryptic digest. The peptides were separated by HPLC and the glycosylated species were identified both by their heterogeneous mass spectra and by an immunoassay. None of the glycopeptides proved to have more than one glycosylation site. The composition of the carbohydrate moieties were calculated by comparing the mass spectra of the glycopeptides before and after enzymic deglycosylation. These results were complemented by data from a carbohydrate composition analysis. In four of the five peptides an α1-3 fucose attached to the asparagine-linked N-acetylglucosamine prevented removal of the glycan by peptide N-glycosidase F; peptide N-glycosidase A removed all carbohydrates from the peptides. To reveal the sequence of the carbohydrate moiety including the linkage positions between the different saccharides, one of the glycopeptides was degraded by specific exoglycosidases. The enzymic degradations by these hydrolases were monitored by mass spectrometry of small aliquots taken at intervals during the reaction. The detailed structure of this one glycan in conjunction with the respective mass spectra and the composition analysis were used to infer the structure of the other four glycans. All glycans of the KBPase have a complex-type xylose-containing structure with four of the five having an additional fucose.

  NCBI PubMed ID: 8125089
  Publication DOI: 10.1111/j.1432-1033.1994.tb18628.x
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Institutions: Institut für Botanik, Westfälische Wilhelms-Universität, Münster, Germany, Institut für Anorganische Chemie, Westfälische Wilhelms-Universität, Münster, Germany, Institut für Biochemie, Westfälische Wilhelms-Universität, Münster, Germany, Institut fur Medizinische Physik, Westfälische Wilhelms-Universität, Münster, Germany
  Methods: GC-MS, GC, MALDI-MS, enzymatic digestion, RP-HPLC, trypsinolysis
  
   
  
  Phaseolus vulgaris
  CSDB ID 124448 (all data & tools)
• Article ID: 10518
  Priem B, Morvan H, Gross KC "Unconjugated N-glycans as a new class of plant oligosaccharins" - Biochemical Society Transactions 22 (1994) 398-402
  
  NCBI PubMed ID: 7958333
  Publication DOI: 10.1042/bst0220398
  Journal NLM ID: 7506897
  Institutions: Centre de Recherches sur les Macromolécules Végétales, CNRS, associé à l'Université J. Fourier, Grenoble, France, Laboratoire de Biologie Cellulaire Végétale et Valorisation des Espèces Ligneuses, 123 rue Albert Thomas, Université de Limoges, Limoges, France, Horticultural Crops Quality Laboratory, USDA/ARS, BARC-W, Bldg. 002, Beltsville, Maryland 20705, U.S.A.
  
   
  
  Silene alba
  CSDB ID 106795 (all data & tools)
• Article ID: 10529
  Kamerling JP "Xylose-containing carbohydrate chains derived from N-glycoproteins" - Pure and Applied Chemistry 63 (1991) 465-472
  

  Xylose-containing N-linked carbohydrate chains are integral parts of certain plant and animal glycoproteins. In all of the known structures, p-D-xylose is 1-2-linked to p-D-mannose of the trimannosyl-N,N'-diacetylchitobiose unit. If a-L-fucose is present at the asparagine-linked N-acetyl-D-glucosamine, then there are differences in the sites of its attachment, namely, a1-3- or a1-6-linked, depending on the biological origin. The a-D-mannose residues can be substituted with additional monosaccharides or 3-0-methylated. The state of the art with respect to structural analysis, organic synthesis, conformational analysis, biosynthesis, lectin binding, and immunological aspects is reviewed.

  Publication DOI: 10.1351/pac199163040465
  Journal NLM ID: 0376514
  Publisher: Oxford: Blackwell Scientific Publications
  Institutions: Bijvoet Center, Department of Bio-Organic Chemistry, Utrecht University, Utrecht, The Netherlands
  
   
  
  Acer pseudoplatanus, Richadella dulcifica, Erythrina, Sophora japonica, Lonchocarpus capassa, Armoracia rusticana, Caesalpinia pulcherrima, Artocarpus intergrifolia, Clerodendron trichotomum, Silene alba
  CSDB ID 148083 (all data & tools)
• Article ID: 10988
  McManus MT, McKeating J, Secher DS, Osborne DJ, Ashford D, Dwek RA, Rademacher TW "Identification of a monoclonal antibody to abscission tissue that recognizes xylose/fucose-containing N-linked oligosaccharides from higher plants" - Planta 175 (1988) 506-512
  
  Journal NLM ID: 1250576
  Publisher: Berlin, New York, Springer
  
   
  
  Sambucus nigra
  CSDB ID 147142 (all data & tools)