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1. Compound ID: 17003
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a-D-Manp-(1-3)-+
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a-D-Manp-(1-6)-+ |
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a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc |
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Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_144983,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_187201,IEDB_429156,IEDB_548907,IEDB_857734,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85
The structure is contained in the following publication(s):
- Article ID: 6606
Chiba Y, Yamagata Y, Nakajima T, Ichishima E "A new high-mannose type N-linked oligosaccharide from Aspergillus carboxypeptidase" -
Bioscience, Biotechnology, and Biochemistry 56 (1992) 1371-1372
Journal NLM ID: 9205717Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
- Article ID: 6615
Takayanagi T, Kushida K, Idonuma K, Ajisaka K "Novel N-linked oligo-mannose type oligosaccharides containing an a-D-galactofuranosyl linkage found in a-D-galactosidase from Aspergillus niger" -
Glycoconjugate Journal 9 (1992) 229-234
Structures of oligosaccharides from Aspergillus niger α-D-galactosidase [EC 3.2.1.22] were studied. Purified α-D-galactosidase was treated with N-glycosidase F, and six kinds of oligosaccharides were isolated by gel chromatography and anion-exchange chromatography. The structures of the oligosaccharides were determined by 1H-NMR and compositional analysis to be Man5GlcNAc2, Man6GlcNAc2, Man9GlcNAc2, GlcMan9GlcNAc2, GalMan4GlcNAc2 and GalMan5GlcNAc2. From mild acid hydrolysis, methylation analysis and ROESY spectral analysis, it was ascertained that the galactosyl residue in two oligosaccharides was in the furanose form and was bound to mannose at the nonreducing end with an α 1-2 linkage (GalfMan4GlcNAc2 and GalfMan5GlcNAc2).
NCBI PubMed ID: 1336999Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Institutions: Meiji Institute of Health Science, Meiji Milk Products Co. Ltd., Odawara, Japan
- Article ID: 6648
Ohta M, Emi S, Iwamoto H, Hirose J, Hiromi K, Itoh H, Shin T, Murao S, Matsuura F "Novel b-D-galactofuranose-containing high-mannose type oligosaccharides in ascorbate oxidase from Acremonium sp. HI-25" -
Bioscience, Biotechnology, and Biochemistry 60 (1996) 1123-1130
Journal NLM ID: 9205717Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
Methods: 1H NMR, FAB-MS
- 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: 1368642Journal NLM ID: 0370452WWW link: http://ci.nii.ac.jp/naid/110006324732Publisher: Tokyo: Agricultural Chemical Society Of Japan
Institutions: Department of Agricultural Sciences, Faculty of Agriculture, Okayama University, Japan
Methods: 1H NMR, HPLC, enzymatic digestion, pyridylamination
- 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: 1368297Journal NLM ID: 9205717Publisher: 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
- 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: 1587803Journal NLM ID: 0376600Publisher: 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
- Article ID: 10245
Nilsen BM, Sletten K, Smestad Paulsen B, O'Neill M, van Halbeek H "Structural analysis of the glycoprotein allergen Art v II from the pollen of mugwort (Artemisia vulgaris L.)" -
Journal of Biological Chemistry 266 (1991) 2660-2668
The glycoprotein allergen Art v II, from the pollen of mugwort (Artemisia vulgaris L.) was treated with peptide:N-glycosidase F (PNGase F) to release asparagine-linked oligosaccharides. The oligosaccharides were isolated by gel permeation chromatography and their structures determined by 500-MHz 1H NMR spectroscopy, fast atom bombardment-mass spectrometry, and high-pH anion-exchange chromatography. The high-mannose oligosaccharides Man5GlcNAc2, Man6GlcNAc2, Man7GlcNAc2, Man8GlcNAc2, and Man9GlcNAc2 were present in the ratios 2:49:19:24:6 and accounted for all the asparagine-linked oligosaccharides released from Art v II by PNGase F. The NH2-terminal amino acid sequences of Art v II and of four peptides generated by cyanogen bromide (CNBr) cleavage of deglycosylated Art v II were determined. The first 30 amino acid residues of Art v II did not contain any potential N-glycosylation sites. One potential N-glycosylation site was identified in one of the CNBr fragments. The native protein conformation was shown by enzyme-linked immunosorbent assay inhibition assays to be essential for the binding of rabbit IgG to Art v II and for the binding of human IgE to the major IgE-binding epitope(s) in this allergen. At least one minor IgE-binding epitope still bound IgE after denaturation of the allergen. Removal of the high-mannose chains from denatured Art v II had no significant effect on the binding of human IgE to the minor IgE-binding epitope(s).
NCBI PubMed ID: 1703533Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Department of Pharmacy, University of Oslo, Norway, Complex Carbohydrate Research Center, Department of Biochemistry, University of Georgia, Athens, Georgia, USA
Methods: 1H NMR, gel filtration, FAB-MS, SDS-PAGE, ELISA, GLC, HPLC, enzymatic digestion, affinity chromatography, HPAE-PAD, preparative isoelectric focusing, Rocket immunoelectrophoresis
- Article ID: 10990
Sadeh S, Warren CD, Daniel PF, Bugge B, James LF, Jeanloz RW "Characterization of oligosaccharides from the urine of loco-intoxicated sheep" -
FEBS Letters 163 (1983) 104-109
Two major oligosaccharides were isolated by preparative HPLC from the urine of a locoweed-fed sheep. Analysis by gas-liquid chromatography and mass-spectrometry indicated compositions of (Man)4(GlcNAc)2 and (Man)5(GlcNAc)2, respectively. Structures were determined by digestion with α-D-mannosidase and endo-β-N-acetylglucosaminidases D and H, and comparison of the products by HPLC with synthetic standards, and oligosaccharides isolated from human mannosidosis urine. Incubation with an exo-β-N-acetylglucosaminidase was without effect.
oligosaccharide, structure, sheep locoweed, urine
NCBI PubMed ID: 6628681Publication DOI: 7/2/201310.1016/0014-5793(83)81173-9Journal NLM ID: 0155157Publisher: Elsevier
Methods: GC, HPLC, CI/IE-MS
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2. Compound ID: 17126
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a-D-Manp-(1-3)-+
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a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_164174,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85
The structure is contained in the following publication(s):
- Article ID: 6648
Ohta M, Emi S, Iwamoto H, Hirose J, Hiromi K, Itoh H, Shin T, Murao S, Matsuura F "Novel b-D-galactofuranose-containing high-mannose type oligosaccharides in ascorbate oxidase from Acremonium sp. HI-25" -
Bioscience, Biotechnology, and Biochemistry 60 (1996) 1123-1130
Journal NLM ID: 9205717Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
Methods: 1H NMR, FAB-MS
- 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: 1368642Journal NLM ID: 0370452WWW link: http://ci.nii.ac.jp/naid/110006324732Publisher: Tokyo: Agricultural Chemical Society Of Japan
Institutions: Department of Agricultural Sciences, Faculty of Agriculture, Okayama University, Japan
Methods: 1H NMR, HPLC, enzymatic digestion, pyridylamination
- 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: 1368297Journal NLM ID: 9205717Publisher: 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
- Article ID: 10990
Sadeh S, Warren CD, Daniel PF, Bugge B, James LF, Jeanloz RW "Characterization of oligosaccharides from the urine of loco-intoxicated sheep" -
FEBS Letters 163 (1983) 104-109
Two major oligosaccharides were isolated by preparative HPLC from the urine of a locoweed-fed sheep. Analysis by gas-liquid chromatography and mass-spectrometry indicated compositions of (Man)4(GlcNAc)2 and (Man)5(GlcNAc)2, respectively. Structures were determined by digestion with α-D-mannosidase and endo-β-N-acetylglucosaminidases D and H, and comparison of the products by HPLC with synthetic standards, and oligosaccharides isolated from human mannosidosis urine. Incubation with an exo-β-N-acetylglucosaminidase was without effect.
oligosaccharide, structure, sheep locoweed, urine
NCBI PubMed ID: 6628681Publication DOI: 7/2/201310.1016/0014-5793(83)81173-9Journal NLM ID: 0155157Publisher: Elsevier
Methods: GC, HPLC, CI/IE-MS
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