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1. Compound ID: 15402
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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-GlcpNAc |
Show graphically |
Structure type: oligomer
Trivial name: carbohydrate chain of the transferrin receptor (TfR)
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: 5964
Mehlert A, Wormald MR, Ferguson MAJ "Modeling of the N-glycosylated transferrin receptor suggests how transferrin binding can occur within the surface coat of Trypanosoma brucei" -
PLoS Pathogens 8(4) (2012) e1002618
The transferrin receptor of bloodstream form Trypanosoma brucei is a heterodimer encoded by expression site associated genes 6 and 7. This low-abundance glycoprotein with a single glycosylphosphatidylinositol membrane anchor and eight potential N-glycosylation sites is located in the flagellar pocket. The receptor is essential for the parasite, providing its only source of iron by scavenging host transferrin from the bloodstream. Here, we demonstrate that both receptor subunits contain endoglycosidase H-sensitive and endoglycosidase H-resistant N-glycans. Lectin blotting of the purified receptor and structural analysis of the released N-glycans revealed oligomannose and paucimannose structures but, contrary to previous suggestions, no poly-N-acetyllactosamine structures were found. Overlay experiments suggest that the receptor can bind to other trypanosome glycoproteins, which may explain this discrepancy. Nevertheless, these data suggest that a current model, in which poly-N-acetyllactosamine glycans are directly involved in receptor-mediated endocytosis in bloodstream form Trypanosoma brucei, should be revised. Sequential endoglycosidase H and peptide-N-glycosidase F treatment, followed by tryptic peptide analysis, allowed the mapping of oligomannose and paucimannose structures to four of the receptor N-glycosylation sites. These results are discussed with respect to the current model for protein N-glycosylation in the parasite. Finally, the glycosylation data allowed the creation of a molecular model for the parasite transferrin receptor. This model, when placed in the context of a model for the dense variant surface glycoprotein coat in which it is embedded, suggests that receptor N-glycosylation may play an important role in providing sufficient space for the approach and binding of transferrin to the receptor, without significantly disrupting the continuity of the protective variant surface glycoprotein coat.
glycoproteins, Glycosylphosphatidylinositol, N-glycosylation, Trypanosoma brucei, variant surface glycoprotein, transferrin receptor
NCBI PubMed ID: 22496646Publication DOI: 10.1371/journal.ppat.1002618Journal NLM ID: 101238921Publisher: San Francisco, CA: Public Library of Science
Correspondence: m.a.j.ferguson@dundee.ac.uk
Institutions: Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dundee, United Kingdom
Methods: SDS-PAGE, HPAEC, Western blotting, radiolabeling, enzymatic digestion, affinity chromatography, HPTLC, LC-MS, LC-MS/MS, lectin blotting
- Article ID: 10881
Hayashi M, Tsuru A, Mitsui T, Takahashi N, Hanzawa H, Arata Y, Akazawa T "Structure and biosynthesis of the xylose-containing carbohydrate moiety of rice α-amylase" -
European Journal of Biochemistry 191 (1990) 287-295
Suspension-cultured cells of rice secrete α-amylase into the culture medium. It has been shown that the mature form of the α-amylase contains xylose-bearing N-linked oligosaccharide: (formula; see text) We demonstrate that suspension-cultured cells of rice secrete α-amylase containing oligomannose-type oligosaccharides in the presence of 1-deoxymannojirimycin or tris(hydroxymethyl)aminomethane. On the other hand, α-amylase purified from germinated rice seedlings contains several kinds of oligomannose-type and N-acetyllactosamine-type oligosaccharides. The processing pathway of oligosaccharide moieties in rice cells is discussed on the basis of a comparison of these oligosaccharides structures.
NCBI PubMed ID: 2143471Publication DOI: 10.1111/j.1432-1033.1990.tb19122.xJournal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Institutions: Research Institute for Biochemical Regulation, School of Agriculture, Nagoya University, Japan, Department of Agricultural Chemistry, Faculty of Agriculture, Niigata University, Japan, Nagoya City University, College of Nursing, Nagoya, Japan, Faculty of Pharmaceutical Science, University of Tokyo, Japan
Methods: 1H NMR, SDS-PAGE, HPLC, enzymatic digestion, pulse-labeling assay
- Article ID: 10989
Kimura Y, Hase S, Kobayashi Y, Kyogoku Y, Ikenaka T, Funatsu G "Structures of sugar chains of Ricinus communis agglutinin" -
Biochimica et Biophysica Acta 966 (1988) 248-256
The structures of sugar chains from Ricinus communis agglutinin were determined. Four glycopeptides were isolated from the lectin according to a published method (Kimura, Y. and Funatsu, G. (1988) Agric. Biol. Chem. 52, in press), and sugar chains of each glycopeptide were liberated by hydrazinolysis. Free amino groups were N-acetylated and the reducing-end residues were coupled with 2-aminopyridine. The resulting pyridylamino derivatives of sugar chains were purified by gel filtration and reversed-phase HPLC. The structures of thus-purified PA-sugar chains were determined by a combination of component analysis, stepwise exoglycosidase digestions, partial acetolysis, and 500 MHz 1H-NMR spectroscopy. These results indicate that R. communis agglutinin contains the sugar chains shown on page 249.
lectin, glycoprotein, Sugar chain structure, Pyridylamino derivative, Sugar chain processing, Ricinus communis agglutinin
Publication DOI: 10.1016/0304-4165(88)90118-3Journal NLM ID: 0217513Publisher: Elsevier
Institutions: Department of Chemistry, Osaka University College of Science, Osaka, Japan, Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka, Japan, Institute for Protein Research, Osaka University, Osaka Japan
Methods: 1H NMR, HPLC, enzymatic digestion, partial acetolysis, CC, RP-HPLC
- Article ID: 10992
Kimura Y, Hase S, Ikenaka T, Funatsu G "Structures of sugar chains of abrin a obtained from Abrus precatorius seeds" -
Biochimica et Biophysica Acta 966 (1988) 150-159
The amino acid sequences around the glycosylation sites and the structures of the sugar chains of abrin a (a lectin derived from Abrus precatorius) were determined. Two glycopeptides were isolated from pronase digests of the B-chain of abrin a after gel filtration and ion-exchange chromatography. The amino acid sequences of these glycopeptides were determined to be Asp-Asn(CHO)-Gly-Thr and Gly-Asn(CHO)-Asn. The sugar chains of each glycopeptide were liberated by hydrazinolysis and then free amino groups were N-acetylated. The reducing-end residues were coupled with 2-aminopyridine and the resulting pyridylamino (PA-) derivatives of sugar chains were purified by reversed-phase HPLC. The structures of the purified PA-sugar chains were estimated by component analysis, comparison of elution positions with those of standard PA-sugar chains by two kinds of HPLC (Hase, S. et al. (1986) J. Biochem. 100, 1–100), stepwise exoglycosidase digestions, and partial acetolysis. Abrin a was shown to contain the following sugar chains [see text].
lectin, Sugar chain structure, abrin, glycopeptide isolation, Abrus precatorius
Publication DOI: 10.1016/0304-4165(88)90138-9Journal NLM ID: 0217513Publisher: Elsevier
Institutions: Department of Chemistry, Osaka University College of Science, Osaka, Japan, Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka, Japan
Methods: HPLC, enzymatic digestion, partial acetolysis, CC, RP-HPLC
- Article ID: 12786
van Ree R, Cabanes-Macheteau M, Akkerdaas J, Milazzo J-P, Loutelier-Bourhis C, Rayon C, Villalba M, Koppelman S, Aalberse R, Rodriguez R, Faye L, Lerouge P "β(1,2)-Xylose and α(1,3)-fucose residues have a strong contribution in IgE binding to plant glycoallergens" -
Journal of Biological Chemistry 275(15) (2000) 11451-11458
Primary structures of the N-glycans of two major pollen allergens (Lol p 11 and Ole e 1) and a major peanut allergen (Ara h 1) were determined. Ole e 1 and Ara h 1 carried high mannose and complex N-glycans, whereas Lol p 11 carried only the complex. The complex structures all had a β(1,2)-xylose linked to the core mannose. Substitution of the proximalN-acetylglucosamine with an α(1,3)-fucose was observed on Lol p 11 and a minor fraction of Ole e 1 but not on Ara h 1. To elucidate the structural basis for IgE recognition of plantN-glycans, radioallergosorbent test analysis with protease digests of the three allergens and a panel of glycoproteins with knownN-glycan structures was performed. It was demonstrated that both α(1,3)-fucose and β(1,2)-xylose are involved in IgE binding. Surprisingly, xylose-specific IgE antibodies that bound to Lol p 11 and bromelain did not recognize closely related xylose-containing structures on horseradish peroxidase, phytohemeagglutinin, Ole e 1, and Ara h 1. On Lol p 11 and bromelain, the core β-mannose is substituted with just an α(1,6)-mannose. On the other xylose-containingN-glycans, an additional α(1,3)-mannose is present. These observations indicate that IgE binding to xylose is sterically hampered by the presence of an α(1,3)-antenna.
allergy, N-glycans, peanut, pollen, IgE binding
NCBI PubMed ID: 10753962Publication DOI: 10.1074/jbc.275.15.11451Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: r_van_ree@clb.nl
Institutions: Department of Allergy, Central Laboratory of The Netherlands Red Cross Blood Transfusion Service and Laboratory for Experimental and Clinical Immunology, Academic Medical Centre, University of Amsterdam, Amsterdam, The Netherlands, Laboratoire des Transports Intracellulaires, CNRS-ESA 6037, Spectrométrie de Masse Bio-organique, Centre Régional Universitaire de Spectroscopie, Institut Fédératif de Recherche Multidisciplinaire sur les Peptides 23, Université de Rouen, Mont Saint Aignan, France, Departamento de Bioquímica y Biología Molecular I, Facultad de Química, Universidad Complutense, Madrid, Spain, Toegepast Natuurwetenschappelijk Onderzoek Nutrition and Food Research Institute, Zeist, The Netherlands
Methods: biological assays
Expand this compound
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2. Compound ID: 15403
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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a-D-Manp-(1-6)-+ |
| |
a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc |
Show graphically |
Structure type: oligomer
Trivial name: carbohydrate chain of the transferrin receptor (TfR)
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_143632,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_136,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85
The structure is contained in the following publication(s):
- Article ID: 5964
Mehlert A, Wormald MR, Ferguson MAJ "Modeling of the N-glycosylated transferrin receptor suggests how transferrin binding can occur within the surface coat of Trypanosoma brucei" -
PLoS Pathogens 8(4) (2012) e1002618
The transferrin receptor of bloodstream form Trypanosoma brucei is a heterodimer encoded by expression site associated genes 6 and 7. This low-abundance glycoprotein with a single glycosylphosphatidylinositol membrane anchor and eight potential N-glycosylation sites is located in the flagellar pocket. The receptor is essential for the parasite, providing its only source of iron by scavenging host transferrin from the bloodstream. Here, we demonstrate that both receptor subunits contain endoglycosidase H-sensitive and endoglycosidase H-resistant N-glycans. Lectin blotting of the purified receptor and structural analysis of the released N-glycans revealed oligomannose and paucimannose structures but, contrary to previous suggestions, no poly-N-acetyllactosamine structures were found. Overlay experiments suggest that the receptor can bind to other trypanosome glycoproteins, which may explain this discrepancy. Nevertheless, these data suggest that a current model, in which poly-N-acetyllactosamine glycans are directly involved in receptor-mediated endocytosis in bloodstream form Trypanosoma brucei, should be revised. Sequential endoglycosidase H and peptide-N-glycosidase F treatment, followed by tryptic peptide analysis, allowed the mapping of oligomannose and paucimannose structures to four of the receptor N-glycosylation sites. These results are discussed with respect to the current model for protein N-glycosylation in the parasite. Finally, the glycosylation data allowed the creation of a molecular model for the parasite transferrin receptor. This model, when placed in the context of a model for the dense variant surface glycoprotein coat in which it is embedded, suggests that receptor N-glycosylation may play an important role in providing sufficient space for the approach and binding of transferrin to the receptor, without significantly disrupting the continuity of the protective variant surface glycoprotein coat.
glycoproteins, Glycosylphosphatidylinositol, N-glycosylation, Trypanosoma brucei, variant surface glycoprotein, transferrin receptor
NCBI PubMed ID: 22496646Publication DOI: 10.1371/journal.ppat.1002618Journal NLM ID: 101238921Publisher: San Francisco, CA: Public Library of Science
Correspondence: m.a.j.ferguson@dundee.ac.uk
Institutions: Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dundee, United Kingdom
Methods: SDS-PAGE, HPAEC, Western blotting, radiolabeling, enzymatic digestion, affinity chromatography, HPTLC, LC-MS, LC-MS/MS, lectin blotting
- Article ID: 10881
Hayashi M, Tsuru A, Mitsui T, Takahashi N, Hanzawa H, Arata Y, Akazawa T "Structure and biosynthesis of the xylose-containing carbohydrate moiety of rice α-amylase" -
European Journal of Biochemistry 191 (1990) 287-295
Suspension-cultured cells of rice secrete α-amylase into the culture medium. It has been shown that the mature form of the α-amylase contains xylose-bearing N-linked oligosaccharide: (formula; see text) We demonstrate that suspension-cultured cells of rice secrete α-amylase containing oligomannose-type oligosaccharides in the presence of 1-deoxymannojirimycin or tris(hydroxymethyl)aminomethane. On the other hand, α-amylase purified from germinated rice seedlings contains several kinds of oligomannose-type and N-acetyllactosamine-type oligosaccharides. The processing pathway of oligosaccharide moieties in rice cells is discussed on the basis of a comparison of these oligosaccharides structures.
NCBI PubMed ID: 2143471Publication DOI: 10.1111/j.1432-1033.1990.tb19122.xJournal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Institutions: Research Institute for Biochemical Regulation, School of Agriculture, Nagoya University, Japan, Department of Agricultural Chemistry, Faculty of Agriculture, Niigata University, Japan, Nagoya City University, College of Nursing, Nagoya, Japan, Faculty of Pharmaceutical Science, University of Tokyo, Japan
Methods: 1H NMR, SDS-PAGE, HPLC, enzymatic digestion, pulse-labeling assay
- Article ID: 10989
Kimura Y, Hase S, Kobayashi Y, Kyogoku Y, Ikenaka T, Funatsu G "Structures of sugar chains of Ricinus communis agglutinin" -
Biochimica et Biophysica Acta 966 (1988) 248-256
The structures of sugar chains from Ricinus communis agglutinin were determined. Four glycopeptides were isolated from the lectin according to a published method (Kimura, Y. and Funatsu, G. (1988) Agric. Biol. Chem. 52, in press), and sugar chains of each glycopeptide were liberated by hydrazinolysis. Free amino groups were N-acetylated and the reducing-end residues were coupled with 2-aminopyridine. The resulting pyridylamino derivatives of sugar chains were purified by gel filtration and reversed-phase HPLC. The structures of thus-purified PA-sugar chains were determined by a combination of component analysis, stepwise exoglycosidase digestions, partial acetolysis, and 500 MHz 1H-NMR spectroscopy. These results indicate that R. communis agglutinin contains the sugar chains shown on page 249.
lectin, glycoprotein, Sugar chain structure, Pyridylamino derivative, Sugar chain processing, Ricinus communis agglutinin
Publication DOI: 10.1016/0304-4165(88)90118-3Journal NLM ID: 0217513Publisher: Elsevier
Institutions: Department of Chemistry, Osaka University College of Science, Osaka, Japan, Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka, Japan, Institute for Protein Research, Osaka University, Osaka Japan
Methods: 1H NMR, HPLC, enzymatic digestion, partial acetolysis, CC, RP-HPLC
- Article ID: 10992
Kimura Y, Hase S, Ikenaka T, Funatsu G "Structures of sugar chains of abrin a obtained from Abrus precatorius seeds" -
Biochimica et Biophysica Acta 966 (1988) 150-159
The amino acid sequences around the glycosylation sites and the structures of the sugar chains of abrin a (a lectin derived from Abrus precatorius) were determined. Two glycopeptides were isolated from pronase digests of the B-chain of abrin a after gel filtration and ion-exchange chromatography. The amino acid sequences of these glycopeptides were determined to be Asp-Asn(CHO)-Gly-Thr and Gly-Asn(CHO)-Asn. The sugar chains of each glycopeptide were liberated by hydrazinolysis and then free amino groups were N-acetylated. The reducing-end residues were coupled with 2-aminopyridine and the resulting pyridylamino (PA-) derivatives of sugar chains were purified by reversed-phase HPLC. The structures of the purified PA-sugar chains were estimated by component analysis, comparison of elution positions with those of standard PA-sugar chains by two kinds of HPLC (Hase, S. et al. (1986) J. Biochem. 100, 1–100), stepwise exoglycosidase digestions, and partial acetolysis. Abrin a was shown to contain the following sugar chains [see text].
lectin, Sugar chain structure, abrin, glycopeptide isolation, Abrus precatorius
Publication DOI: 10.1016/0304-4165(88)90138-9Journal NLM ID: 0217513Publisher: Elsevier
Institutions: Department of Chemistry, Osaka University College of Science, Osaka, Japan, Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka, Japan
Methods: HPLC, enzymatic digestion, partial acetolysis, CC, RP-HPLC
- Article ID: 12786
van Ree R, Cabanes-Macheteau M, Akkerdaas J, Milazzo J-P, Loutelier-Bourhis C, Rayon C, Villalba M, Koppelman S, Aalberse R, Rodriguez R, Faye L, Lerouge P "β(1,2)-Xylose and α(1,3)-fucose residues have a strong contribution in IgE binding to plant glycoallergens" -
Journal of Biological Chemistry 275(15) (2000) 11451-11458
Primary structures of the N-glycans of two major pollen allergens (Lol p 11 and Ole e 1) and a major peanut allergen (Ara h 1) were determined. Ole e 1 and Ara h 1 carried high mannose and complex N-glycans, whereas Lol p 11 carried only the complex. The complex structures all had a β(1,2)-xylose linked to the core mannose. Substitution of the proximalN-acetylglucosamine with an α(1,3)-fucose was observed on Lol p 11 and a minor fraction of Ole e 1 but not on Ara h 1. To elucidate the structural basis for IgE recognition of plantN-glycans, radioallergosorbent test analysis with protease digests of the three allergens and a panel of glycoproteins with knownN-glycan structures was performed. It was demonstrated that both α(1,3)-fucose and β(1,2)-xylose are involved in IgE binding. Surprisingly, xylose-specific IgE antibodies that bound to Lol p 11 and bromelain did not recognize closely related xylose-containing structures on horseradish peroxidase, phytohemeagglutinin, Ole e 1, and Ara h 1. On Lol p 11 and bromelain, the core β-mannose is substituted with just an α(1,6)-mannose. On the other xylose-containingN-glycans, an additional α(1,3)-mannose is present. These observations indicate that IgE binding to xylose is sterically hampered by the presence of an α(1,3)-antenna.
allergy, N-glycans, peanut, pollen, IgE binding
NCBI PubMed ID: 10753962Publication DOI: 10.1074/jbc.275.15.11451Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: r_van_ree@clb.nl
Institutions: Department of Allergy, Central Laboratory of The Netherlands Red Cross Blood Transfusion Service and Laboratory for Experimental and Clinical Immunology, Academic Medical Centre, University of Amsterdam, Amsterdam, The Netherlands, Laboratoire des Transports Intracellulaires, CNRS-ESA 6037, Spectrométrie de Masse Bio-organique, Centre Régional Universitaire de Spectroscopie, Institut Fédératif de Recherche Multidisciplinaire sur les Peptides 23, Université de Rouen, Mont Saint Aignan, France, Departamento de Bioquímica y Biología Molecular I, Facultad de Química, Universidad Complutense, Madrid, Spain, Toegepast Natuurwetenschappelijk Onderzoek Nutrition and Food Research Institute, Zeist, The Netherlands
Methods: biological assays
Expand this compound
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3. Compound ID: 16980
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a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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a-D-Manp-(1-3)-+ |
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-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_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_187201,IEDB_187238,IEDB_187239,IEDB_429156,IEDB_540671,IEDB_548907,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85
The structure is contained in the following publication(s):
- Article ID: 6595
Verostek MF, Atkinson PH, Trimble RB "Structure of Saccharomyces cerevisiae alg3,sec18 mutant oligosaccharides" -
Journal of Biological Chemistry 266 (1991) 5547-5551
Asparagine-linked oligosaccharides are synthesized by transfer of Glc3Man9GlcNAc2 from dolichol pyrophosphate to nascent polypeptides. Assembly of the precursor proceeds by highly ordered sequential addition of mannose and glucose to form Glc3Man9GlcNAc2-P-P-dolichol. Yeast mutants in asparagine-linked glycosylation (alg), generated by an 3H-Man suicide technique, were assigned to eight complementation groups which define steps in oligosaccharide-lipid synthesis (Huffaker, T.C., and Robbins, P.W. (1982) J. Biol. Chem. 257, 3203-3210). Alg3 invertase oligosaccharides are resistant to endo-β-N-acetylglucosaminidase H, and the lipid-oligosaccharide pool yields Man5Glc-NAc2, suggesting its structure may be that from mammalian cells lacking Man-P-dolichol (Chapman, A., et al. (1980) J. Biol. Chem. 255, 4441-4446). To test this supposition, the endoplasmic reticulum form of invertase derepressed in alg3,sec18 yeast at 37 degrees C was isolated as a source of oligosaccharides whose processing beyond glucose and/or mannose trimming, if involved, would be prevented. Man8GlcNAc2 and Man5GlcNAc2 were released by peptide-N-glycosidase F from alg3,sec18 invertase in a 1:5 molar ratio. 1H NMR spectroscopy revealed Man8GlcNAc2 to be the α-1,2-mannosidase-trimming product described earlier (Byrd, J. C., Tarentino, A. L., Maley, F., Atkinson, P. H., and Trimble, R. B. (1982) J. Biol. Chem. 257, 14657-14666), while Man5GlcNAc2 was Man α-1, 2Man α-1,2Man α-1,3(Man α-1,6)Man β-1,4GlcNAc β-1,4GlcNAc. This provides a structural proof for the lipid-linked Man5GlcNAc2 originally proposed from enzymatic and chemical analyses of the radiolabeled mammalian precursor. Experimental evidence indicates that, unlike the mammalian cell mutants which are unable to synthesize Man-P-dolichol, alg3 yeast accumulate Man5GlcNAc2-P-P-dolichol due to a defective α-1,3-mannosyltransferase required for the next step in oligosaccharide-lipid elongation.
NCBI PubMed ID: 2005096Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509
Methods: 1H NMR, gel filtration, methylation analysis, PNGase F digestion, Smith-periodate oxidation
- Article ID: 6642
Takayanagi T, Kimura A, Chiba S, Ajisaka K "Novel structures of N-linked high-mannose type oligosaccharides containing a-D-galactofuranosyl linkages in Aspergillus niger a-D-glucosidase" -
Carbohydrate Research 256 (1994) 149-158
Seven oligosaccharides were isolated from α-D-glucosidase (EC 3.2.1.20) from Aspergillus niger, and the structures of these oligosaccharides were studied by 1H NMR spectroscopy. After treatment of the α-D-glucosidase with N-glycosidase F, seven major oligosaccharide peaks were detected by Dionex anion-exchange HPLC. The structures corresponding to the three peaks OS-1, OS-2, and OS-4 were determined to be Man8GlcNAc2, Man9GlcNAc2, and GlcMan9GlcNAc2, respectively, from 1H NMR spectra of the isolated fractions. Each of the four oligosaccharides OS-5, OS-6, OS-7-1, and OS-7-2 contained an α-D-galactofuranosyl residue (Galf) linked to Man(A) via an α-(1→2)-linkage. OS-7 was found to consist of two oligosaccharides. The structures of these four oligosaccharides were determined to be GalfMan5GlcNAc2, GalfMan6GlcNAc2, GalfMan7GlcNAc2, and GalfMan8GlcNAc2 by 1H NMR spectroscopy and compositional analysis. The Galf structure of GalfMan5GlcNAc2 was found to be identical to that of an oligosaccharide previously isolated from the α-D-galactosidase of the same strain. The structure of OS-3 remains undetermined.
NCBI PubMed ID: 8194071Journal NLM ID: 0043535Publisher: Elsevier
Institutions: Meiji Institute of Health Science, Meiji Milk Products Co., Ltd., Odawara, Japan
Methods: 1H NMR, gel filtration, SDS-PAGE, HPLC, enzymatic digestion, Western blot, proteolysis
- 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: 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)90139-0Journal NLM ID: 0217513Publisher: 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
- 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: 10984
Navazio L, Baldan B, Mariani P, Gerwig GJ, Vliegenthart JFG "Primary structure of the N-linked carbohydrate chains of Calreticulin from spinach leaves" -
Glycoconjugate Journal 13 (1996) 977-983
Calreticulin is a multifunctional Ca(2+)-binding protein of the endoplasmic reticulum of most eukaryotic cells. The 56 kDa Calreticulin glycoprotein isolated from spinach (Spinacia oleracea L.) leaves was N-deglycosylated by PNGase-F digestion. The carbohydrate moiety was isolated by gel permeation chromatography and purified by high-pH anion-exchange chromatography. The fractions were investigated by 500 MHz 1H-NMR spectroscopy, in combination with monosaccharide analysis and fast-atom bombardment-mass spectrometry. The following carbohydrate structure could be established as the major component (Man8GlcNAc2): (sequence see text) Heterogeneity was demonstrated by the presence of two minor components being Man7GlcNAc2 lacking a terminal residue (D1 or D3), compared to the major component. A cross-reactivity with an antibody against the endoplasmic reticulum retention signal HDEL was also found.
NCBI PubMed ID: 8981089Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Institutions: Department of Biology, University of Padova, Italy
Methods: 1H NMR
Expand this compound
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4. Compound ID: 17030
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
|
a-D-Manp-(1-6)-+ |
| |
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_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_143632,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_136,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85
The structure is contained in the following publication(s):
- 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: 6805
Flores-Carreon A, Hixson SH, Gomez A, Shao MC, Krudy G, Rosevear PR, Wold F "The processing of N-linked glycans in yeast. Mutually exclusive steps in the processing of a Man6 derivative by yeast membrane preparations" -
Journal of Biological Chemistry 265 (1990) 754-759
When a derivatized oligosaccharide isolated from ovalbumin and containing 6 mannose residues was incubated with yeast membranes and GDP-mannose, two sets of products were obtained, a high molecular weight one containing about 25 mannose residues and a low molecular weight one consisting of compounds with 7, 8, and 9 mannose residues, respectively. When the low molecular weight products were reincubated with the yeast membranes and GDP-mannose, no further mannose incorporation was observed, showing that these compounds must be of the wrong structure as substrates for yeast glycan processing enzymes. The structures were investigated by 1H NMR spectroscopy. The high molecular weight products contained an outer chain of an average length of 18 1----6-linked mannose residues attached to a core structure made up of the original 6 mannose residues with one additional 1----2-linked mannose added. The low molecular weight product with 8 mannose residues was deduced to contain a terminal 1----6-linked mannose (on the 1----6 arm) substituted by mannose at the 2-position, and the ones with 7 and 9 mannose residues were identified as having an additional 1----3-linked mannose on the starting Man6 substrate and on the Man8 product, respectively. The results lend further support to the picture that the processing steps must occur in proper sequence for specific products to form.
NCBI PubMed ID: 2404010Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston 77225
- Article ID: 9828
Oxley D, Munro SLA, Craik DJ, Bacic A "structure and distribution of N-glycans on the S7-allele stylar self-incompatibility ribonuclease of Nicotiana alata" -
Journal of Biochemistry 123 (1998) 978-983
S-RNases are the stylar products of the self-incompatibility (S)-locus in solanaceous plants (including Nicotiana alata), and as such, are involved in the prevention of self-pollination. All cDNA sequences of S-RNase products of functional S-alleles contain potential N-glycosylation sites, with one site being conserved in all cases, suggesting that N-glycosylation is important in self-incompatibility. In this study, we report on the structure and localization of the N-glycans on the S7-allele RNase of N. alata. A total of nine N-glycans, belonging to the high-mannose- and xylosylated hybrid-classes, were identified and characterized by a combination of electrospray-ionization mass-spectrometry (ESI-MS), 1H-NMR spectroscopy, and methylation analyses. The glycosylation pattern of individual glycosylation sites was determined by ESI-MS of the glycans released from isolated chymotryptic glycopeptides. All three N-glycosylation sites showed microheterogeneity and each had a unique complement of N-glycans. The N-glycosylation pattern of the S7-RNase is significantly different to those of the S1- and S2-RNases.
microheterogeneity, N-glycan, Nicotiana alata, ribonuclease, self-incompatibility.
NCBI PubMed ID: 9562634Journal NLM ID: 0376600Publisher: Japanese Biochemical Society
Correspondence: d.oxley@botany.unimelb.edu
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Parkville, Victoria 3052, Australia, Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Parkville, Victoria 3052, Australia.
Methods: 1H NMR, IR, SDS-PAGE, ESI-MS, HPLC, methylation analysis, chymotrypsin digestion, peptide sequencing
- 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)90139-0Journal NLM ID: 0217513Publisher: 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
- 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
Expand this compound
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5. Compound ID: 17243
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
|
a-D-Manp-(1-3)-+ |
| |
a-D-Manp-(1-2)-a-D-Manp-(1-6)-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_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141831,IEDB_143632,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_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,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: 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)90139-0Journal NLM ID: 0217513Publisher: 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
- 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
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6. Compound ID: 24297
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a-D-Manp-(1-3)-+ a-L-Fucp-(1-3)-+
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b-D-Xylp-(1-2)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc
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a-D-Manp-(1-6)-+ |
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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
The structure is contained in the following publication(s):
- 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: 8243456Journal NLM ID: 0107600Publisher: 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
- 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)90139-0Journal NLM ID: 0217513Publisher: 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
- 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: 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: 2335505Journal NLM ID: 2985121RPublisher: 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
- 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: 1705547Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Department of Biotechnology, Faculty of Engineering, Sangyo University, Japan
- 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: 1498421Journal NLM ID: 9104124Publisher: 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
- 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: 8125089Publication DOI: 10.1111/j.1432-1033.1994.tb18628.xJournal NLM ID: 0107600Publisher: 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
- 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: 7958333Publication DOI: 10.1042/bst0220398Journal NLM ID: 7506897Institutions: 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.
- 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/pac199163040465Journal NLM ID: 0376514Publisher: Oxford: Blackwell Scientific Publications
Institutions: Bijvoet Center, Department of Bio-Organic Chemistry, Utrecht University, Utrecht, The Netherlands
- 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: 1250576Publisher: Berlin, New York, Springer
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7. Compound ID: 24728
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a-L-Rhap-(1-2)-b-D-Galp-(1-2)-b-D-GlcpA6Me-(1-3)-Subst
Subst = sophoradiol = SMILES C[C@]12CC{3}[C@H](O)C(C)(C)[C@@H]1CC[C@]3(C)[C@@H]2CC=C4[C@@]3(C)CC[C@]5(C)[C@H]4CC(C)(C)C{22}[C@H]5O |
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Structure type: oligomer
Trivial name: kaikosaponin III, kaikasaponin
Compound class: saponin glycoside
Contained glycoepitopes: IEDB_115136,IEDB_136044,IEDB_136105,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_190606,IEDB_225177,IEDB_423153,IEDB_885823,SB_165,SB_166,SB_187,SB_195,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 10145
Kitagawa I, Taniyama T, Hong WW, Hori K, Yoshikawa M "Saponin and sapogenol. XLV. Structures of kaikasaponins I, II, and III from sophorae flos, the buds of Sophora japonica L" -
Yakugaku Zasshi = Journal of the Pharmaceutical Society of Japan [Japanese] 108 (1988) 538-546
Three new glucuronide-saponins, named kaikasaponin I (7), kaikasaponin II (8), and kaikasaponin III (9), were isolated from Sophorae Flos, the buds of Sophora japonica L. (Leguminosae), together with five known glucuronide-saponins soyasaponin I (6), soyasaponin III (4), azukisaponin I (2), azukisaponin II (3), and azukisaponin V (5). By use of the photochemical degradation method, which is one of selective cleavage-methods for the glucuronide linkage in glucuronide-saponins, and on the basis of chemical and spectral evidence, the structures of kaikasaponins I, II, and III have been determined as 3-O-[β-D-galactopyranosyl-(1→2)-β-D-glucuronopyranosyl]sophoradiol (7), 3-O-[α-L-rhamnopyranosyl-(l→2)-β-D-glucopyranosyl-(l→2)-β-D-glucuronopyranosyl]sophoradiol (8), and 3-O-[α-L-rhamnopyranosyl-(1→2)-β-D-galactopyranosyl-(1→2)-β-D-glucuronopyranosyl]sophoradiol (9), respectively. In the course of ^<13>C nuclear magnetic resonance spectral analysis of these kaikasaponins, it has been noticed that some chemical shifts of carbohydrate carbons close to the sapogenol are affected by the presence of a hydroxyl group in the sapogenol nearby the glucuronide linkage.
Journal NLM ID: 0413613WWW link: http://ci.nii.ac.jp/naid/110003648664Publisher: Tokyo: Nihon Yakugakkai
Institutions: Faculty of Pharmaceutical Sciences, Osaka University, Osaka, japan
Methods: 13C NMR
- Article ID: 10217
Kinjo J, Matsumoto K, Inoue M, Takeshita T, Nohara T "Studies on leguminous plants. Part XIX. A new sapogenol and other constituents in abri semen, the seeds of Abrus precatorius L. I" -
Chemical and Pharmaceutical Bulletin 39 (1991) 116-119
Further study on the chemical constituents of the Abrus species resulted in the isolation of a new sapogenol, abrisapogenol J (1), from the methanolysate of the seeds for Abrus precatorius L., together with sophoradiol (4), its 22-O-acetate (2) and hederagenin methyl ester (5). The structure of 1 has been elucidated to be 3β,22β-dihydroxy-11-oxoolean-13(18)-ene by the use of hetero unclear multiple bonds correlation (HMBC) spectroscopy. In addition, various compounds, trimethyl tryptophan dipolar ion (3), kaikasaponin III methyl ester (6), abrine (7), abrusin (8) and its 2"-O-apioside (9) were obtained from the methanolic extract.
Journal NLM ID: 0377775WWW link: http://ci.nii.ac.jp/naid/110003628862Publisher: Pharmaceutical Society Of Japan
Institutions: Faculty of Pharmaceutical Sciences, Kumamoto University, Japan
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8. Compound ID: 27077
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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a-D-Manp-(1-3)-+ |
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc |
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Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141831,IEDB_143632,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_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85
The structure is contained in the following publication(s):
- Article ID: 10881
Hayashi M, Tsuru A, Mitsui T, Takahashi N, Hanzawa H, Arata Y, Akazawa T "Structure and biosynthesis of the xylose-containing carbohydrate moiety of rice α-amylase" -
European Journal of Biochemistry 191 (1990) 287-295
Suspension-cultured cells of rice secrete α-amylase into the culture medium. It has been shown that the mature form of the α-amylase contains xylose-bearing N-linked oligosaccharide: (formula; see text) We demonstrate that suspension-cultured cells of rice secrete α-amylase containing oligomannose-type oligosaccharides in the presence of 1-deoxymannojirimycin or tris(hydroxymethyl)aminomethane. On the other hand, α-amylase purified from germinated rice seedlings contains several kinds of oligomannose-type and N-acetyllactosamine-type oligosaccharides. The processing pathway of oligosaccharide moieties in rice cells is discussed on the basis of a comparison of these oligosaccharides structures.
NCBI PubMed ID: 2143471Publication DOI: 10.1111/j.1432-1033.1990.tb19122.xJournal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Institutions: Research Institute for Biochemical Regulation, School of Agriculture, Nagoya University, Japan, Department of Agricultural Chemistry, Faculty of Agriculture, Niigata University, Japan, Nagoya City University, College of Nursing, Nagoya, Japan, Faculty of Pharmaceutical Science, University of Tokyo, Japan
Methods: 1H NMR, SDS-PAGE, HPLC, enzymatic digestion, pulse-labeling assay
- Article ID: 10992
Kimura Y, Hase S, Ikenaka T, Funatsu G "Structures of sugar chains of abrin a obtained from Abrus precatorius seeds" -
Biochimica et Biophysica Acta 966 (1988) 150-159
The amino acid sequences around the glycosylation sites and the structures of the sugar chains of abrin a (a lectin derived from Abrus precatorius) were determined. Two glycopeptides were isolated from pronase digests of the B-chain of abrin a after gel filtration and ion-exchange chromatography. The amino acid sequences of these glycopeptides were determined to be Asp-Asn(CHO)-Gly-Thr and Gly-Asn(CHO)-Asn. The sugar chains of each glycopeptide were liberated by hydrazinolysis and then free amino groups were N-acetylated. The reducing-end residues were coupled with 2-aminopyridine and the resulting pyridylamino (PA-) derivatives of sugar chains were purified by reversed-phase HPLC. The structures of the purified PA-sugar chains were estimated by component analysis, comparison of elution positions with those of standard PA-sugar chains by two kinds of HPLC (Hase, S. et al. (1986) J. Biochem. 100, 1–100), stepwise exoglycosidase digestions, and partial acetolysis. Abrin a was shown to contain the following sugar chains [see text].
lectin, Sugar chain structure, abrin, glycopeptide isolation, Abrus precatorius
Publication DOI: 10.1016/0304-4165(88)90138-9Journal NLM ID: 0217513Publisher: Elsevier
Institutions: Department of Chemistry, Osaka University College of Science, Osaka, Japan, Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka, Japan
Methods: HPLC, enzymatic digestion, partial acetolysis, CC, RP-HPLC
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9. Compound ID: 27429
|
b-D-Xylp-(1-2)-+
|
a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc
|
a-D-Manp-(1-3)-+ |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_123886,IEDB_123887,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_164174,IEDB_167188,IEDB_174332,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: 10989
Kimura Y, Hase S, Kobayashi Y, Kyogoku Y, Ikenaka T, Funatsu G "Structures of sugar chains of Ricinus communis agglutinin" -
Biochimica et Biophysica Acta 966 (1988) 248-256
The structures of sugar chains from Ricinus communis agglutinin were determined. Four glycopeptides were isolated from the lectin according to a published method (Kimura, Y. and Funatsu, G. (1988) Agric. Biol. Chem. 52, in press), and sugar chains of each glycopeptide were liberated by hydrazinolysis. Free amino groups were N-acetylated and the reducing-end residues were coupled with 2-aminopyridine. The resulting pyridylamino derivatives of sugar chains were purified by gel filtration and reversed-phase HPLC. The structures of thus-purified PA-sugar chains were determined by a combination of component analysis, stepwise exoglycosidase digestions, partial acetolysis, and 500 MHz 1H-NMR spectroscopy. These results indicate that R. communis agglutinin contains the sugar chains shown on page 249.
lectin, glycoprotein, Sugar chain structure, Pyridylamino derivative, Sugar chain processing, Ricinus communis agglutinin
Publication DOI: 10.1016/0304-4165(88)90118-3Journal NLM ID: 0217513Publisher: Elsevier
Institutions: Department of Chemistry, Osaka University College of Science, Osaka, Japan, Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka, Japan, Institute for Protein Research, Osaka University, Osaka Japan
Methods: 1H NMR, HPLC, enzymatic digestion, partial acetolysis, CC, RP-HPLC
- Article ID: 10992
Kimura Y, Hase S, Ikenaka T, Funatsu G "Structures of sugar chains of abrin a obtained from Abrus precatorius seeds" -
Biochimica et Biophysica Acta 966 (1988) 150-159
The amino acid sequences around the glycosylation sites and the structures of the sugar chains of abrin a (a lectin derived from Abrus precatorius) were determined. Two glycopeptides were isolated from pronase digests of the B-chain of abrin a after gel filtration and ion-exchange chromatography. The amino acid sequences of these glycopeptides were determined to be Asp-Asn(CHO)-Gly-Thr and Gly-Asn(CHO)-Asn. The sugar chains of each glycopeptide were liberated by hydrazinolysis and then free amino groups were N-acetylated. The reducing-end residues were coupled with 2-aminopyridine and the resulting pyridylamino (PA-) derivatives of sugar chains were purified by reversed-phase HPLC. The structures of the purified PA-sugar chains were estimated by component analysis, comparison of elution positions with those of standard PA-sugar chains by two kinds of HPLC (Hase, S. et al. (1986) J. Biochem. 100, 1–100), stepwise exoglycosidase digestions, and partial acetolysis. Abrin a was shown to contain the following sugar chains [see text].
lectin, Sugar chain structure, abrin, glycopeptide isolation, Abrus precatorius
Publication DOI: 10.1016/0304-4165(88)90138-9Journal NLM ID: 0217513Publisher: Elsevier
Institutions: Department of Chemistry, Osaka University College of Science, Osaka, Japan, Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka, Japan
Methods: HPLC, enzymatic digestion, partial acetolysis, CC, RP-HPLC
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10. Compound ID: 28604
|
b-D-GlcpA-(1-2)-b-D-Glcp-(1-3)-Subst
Subst = hederagenin = SMILES CC1(C)CC[C@]2({28}C(O)=O)CC[C@@]3(C)[C@]4(C)CC[C@@]5([H])[C@](C)({23}CO){3}[C@@H](O)CC[C@]5(C)[C@@]4([H])CC=C3[C@]2([H])C1 |
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Structure type: oligomer
; 833 [M+Na]+
C42H66O15
Trivial name: abrus-saponin I
Compound class: triterpenoid glycoside
Contained glycoepitopes: IEDB_115136,IEDB_140630,IEDB_142488,IEDB_146664,IEDB_423153,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 11318
Ma CM, Nakamura N, Hattori M "Saponins and C-glycosyl flavones from the seeds of Abrus precatorius" -
Chemical and Pharmaceutical Bulletin 46(6) (1998) 982-987
Two new saponins, 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]hederagenin (named abrus-saponin I) and 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]oleanolic acid 28-beta-D-glucopyranosyI ester (abrus-saponin II), and three new flavones, 6-C-beta-D-glucopyranosyl-4',5-dihydroxy-7,8-dimethoxyflavone (precatorin I), 6-C-[beta-D-apiofuranosyl-(1-->2)-beta-D-glucopyranosyl]-4',5-dihydroxy-7,8-dimethoxyflavone (precatorin II), 6-C-[beta-D-apiofuranosyl-(1-->2)-beta-D-glucopyranosyl]4',5-dihydroxy-7-methoxyflavone (precatorin III), were isolated from the seeds of Abrus precatorius L. together with twelve known compounds including a naturally new saponin, 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]oleanolic acid. Their structures were determined on the basis of chemical and spectroscopic methods, In addition, the unusual NMR spectral behavior of the flavone C-glycosides is also discussed.
saponin, Leguminosae, Abrus precatorius, C-glycosyl flavone
Publication DOI: 10.1248/cpb.46.982Journal NLM ID: 0377775Publisher: Pharmaceutical Society Of Japan
Institutions: Research Institute for Wakan-Yaku, Toyama Medical and Pharmaceutical University, Toyama, Japan
Methods: 13C NMR, 1H NMR, methylation, IR, FAB-MS, acid hydrolysis, UV, extraction, optical rotation measurement, reversed-phase chromatography, HMBC, HMQC, COSY, HOHAHA, API-MS
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11. Compound ID: 28605
|
b-D-GlcpA-(1-2)-b-D-Glcp-(1-3)-Subst
Subst = oleanolic acid = SMILES O{3}[C@H]1CC[C@]2(C)[C@@]3([H])CC=C4[C@]5([H])CC(C)(C)CC[C@@]({28}C(O)=O)5CC[C@](C)4[C@@](C)3CC[C@]([H])2C1(C)C |
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Structure type: oligomer
; 817 [M+Na]+
Compound class: triterpenoid glycoside
Contained glycoepitopes: IEDB_115136,IEDB_140630,IEDB_142488,IEDB_146664,IEDB_423153,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 11318
Ma CM, Nakamura N, Hattori M "Saponins and C-glycosyl flavones from the seeds of Abrus precatorius" -
Chemical and Pharmaceutical Bulletin 46(6) (1998) 982-987
Two new saponins, 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]hederagenin (named abrus-saponin I) and 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]oleanolic acid 28-beta-D-glucopyranosyI ester (abrus-saponin II), and three new flavones, 6-C-beta-D-glucopyranosyl-4',5-dihydroxy-7,8-dimethoxyflavone (precatorin I), 6-C-[beta-D-apiofuranosyl-(1-->2)-beta-D-glucopyranosyl]-4',5-dihydroxy-7,8-dimethoxyflavone (precatorin II), 6-C-[beta-D-apiofuranosyl-(1-->2)-beta-D-glucopyranosyl]4',5-dihydroxy-7-methoxyflavone (precatorin III), were isolated from the seeds of Abrus precatorius L. together with twelve known compounds including a naturally new saponin, 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]oleanolic acid. Their structures were determined on the basis of chemical and spectroscopic methods, In addition, the unusual NMR spectral behavior of the flavone C-glycosides is also discussed.
saponin, Leguminosae, Abrus precatorius, C-glycosyl flavone
Publication DOI: 10.1248/cpb.46.982Journal NLM ID: 0377775Publisher: Pharmaceutical Society Of Japan
Institutions: Research Institute for Wakan-Yaku, Toyama Medical and Pharmaceutical University, Toyama, Japan
Methods: 13C NMR, 1H NMR, methylation, IR, FAB-MS, acid hydrolysis, UV, extraction, optical rotation measurement, reversed-phase chromatography, HMBC, HMQC, COSY, HOHAHA, API-MS
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12. Compound ID: 28606
|
b-D-Glcp-(1-28)-+
|
b-D-GlcpA-(1-2)-b-D-Glcp-(1-3)-Subst
Subst = oleanolic acid = SMILES O{3}[C@H]1CC[C@]2(C)[C@@]3([H])CC=C4[C@]5([H])CC(C)(C)CC[C@@]({28}C(O)=O)5CC[C@](C)4[C@@](C)3CC[C@]([H])2C1(C)C |
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Structure type: oligomer
; 979 [M+Na]+
Trivial name: abrus-saponin II
Compound class: triterpenoid glycoside
Contained glycoepitopes: IEDB_115136,IEDB_140630,IEDB_142488,IEDB_146664,IEDB_423153,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 11318
Ma CM, Nakamura N, Hattori M "Saponins and C-glycosyl flavones from the seeds of Abrus precatorius" -
Chemical and Pharmaceutical Bulletin 46(6) (1998) 982-987
Two new saponins, 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]hederagenin (named abrus-saponin I) and 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]oleanolic acid 28-beta-D-glucopyranosyI ester (abrus-saponin II), and three new flavones, 6-C-beta-D-glucopyranosyl-4',5-dihydroxy-7,8-dimethoxyflavone (precatorin I), 6-C-[beta-D-apiofuranosyl-(1-->2)-beta-D-glucopyranosyl]-4',5-dihydroxy-7,8-dimethoxyflavone (precatorin II), 6-C-[beta-D-apiofuranosyl-(1-->2)-beta-D-glucopyranosyl]4',5-dihydroxy-7-methoxyflavone (precatorin III), were isolated from the seeds of Abrus precatorius L. together with twelve known compounds including a naturally new saponin, 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]oleanolic acid. Their structures were determined on the basis of chemical and spectroscopic methods, In addition, the unusual NMR spectral behavior of the flavone C-glycosides is also discussed.
saponin, Leguminosae, Abrus precatorius, C-glycosyl flavone
Publication DOI: 10.1248/cpb.46.982Journal NLM ID: 0377775Publisher: Pharmaceutical Society Of Japan
Institutions: Research Institute for Wakan-Yaku, Toyama Medical and Pharmaceutical University, Toyama, Japan
Methods: 13C NMR, 1H NMR, methylation, IR, FAB-MS, acid hydrolysis, UV, extraction, optical rotation measurement, reversed-phase chromatography, HMBC, HMQC, COSY, HOHAHA, API-MS
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13. Compound ID: 28607
|
b-D-Galp-(1-2)-b-D-GlcpA-(1-3)-Subst
Subst = sophoradiol = SMILES C[C@]12CC{3}[C@H](O)C(C)(C)[C@@H]1CC[C@]3(C)[C@@H]2CC=C4[C@@]3(C)CC[C@]5(C)[C@H]4CC(C)(C)C{22}[C@H]5O |
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Structure type: oligomer
; 803 [M+Na]+
Trivial name: kaikasaponin I
Compound class: glycoside, triterpenoid glycoside
Contained glycoepitopes: IEDB_115136,IEDB_136044,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_190606,IEDB_423153,SB_165,SB_166,SB_187,SB_195,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 11318
Ma CM, Nakamura N, Hattori M "Saponins and C-glycosyl flavones from the seeds of Abrus precatorius" -
Chemical and Pharmaceutical Bulletin 46(6) (1998) 982-987
Two new saponins, 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]hederagenin (named abrus-saponin I) and 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]oleanolic acid 28-beta-D-glucopyranosyI ester (abrus-saponin II), and three new flavones, 6-C-beta-D-glucopyranosyl-4',5-dihydroxy-7,8-dimethoxyflavone (precatorin I), 6-C-[beta-D-apiofuranosyl-(1-->2)-beta-D-glucopyranosyl]-4',5-dihydroxy-7,8-dimethoxyflavone (precatorin II), 6-C-[beta-D-apiofuranosyl-(1-->2)-beta-D-glucopyranosyl]4',5-dihydroxy-7-methoxyflavone (precatorin III), were isolated from the seeds of Abrus precatorius L. together with twelve known compounds including a naturally new saponin, 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]oleanolic acid. Their structures were determined on the basis of chemical and spectroscopic methods, In addition, the unusual NMR spectral behavior of the flavone C-glycosides is also discussed.
saponin, Leguminosae, Abrus precatorius, C-glycosyl flavone
Publication DOI: 10.1248/cpb.46.982Journal NLM ID: 0377775Publisher: Pharmaceutical Society Of Japan
Institutions: Research Institute for Wakan-Yaku, Toyama Medical and Pharmaceutical University, Toyama, Japan
Methods: 13C NMR, 1H NMR, methylation, IR, FAB-MS, acid hydrolysis, UV, extraction, optical rotation measurement, reversed-phase chromatography, HMBC, HMQC, COSY, HOHAHA, API-MS
- Article ID: 12556
Oh S-R, Kinjo J, Shii Y, Ikeda T, Nohara T, Ahn KS, Kim JH, Lee H-K "Effects of triterpenoids from Pueraria lobata on immunohemolysis: β-D-glucuronic acid plays an active role in anticomplementary activity in vitro" -
Planta Medica 66(6) (2000) 506-510
The anticomplementary properties of kaikasaponin III (4) and soyasaponin I (8) from Pueraria lobata and their hydrolytic analogs were investigated in vitro. Diglycosidic saponins [kaikasaponin I (3), soyasaponin III (7)] showed most potent anticomplementary activities, followed by monoglycosidic saponins [soyasapogenol B monoglucuronide (6), sophoradiol monoglucuronide (2)] and triglycosidic saponins [soyasaponin I (8), kaikasaponin III (4)], whereas sophoradiol (1) and soyasapogenol B (5) showed enhancement of hemolysis under the presence of serum on the classical pathway of complement system. But all of them showed very weak or no anticomplementary activities on the alternative pathway of complement system. The anticomplementary activity of the saponins was influenced by the nature of glucuronic acid, where the free acid forms (-COOH) showed much more potent activity than the sodium salt forms (-COO-Na+) or methyl ester forms (-COOCH3), and the reduced forms (-CH2OH) decreased the activity significantly.
Leguminosae, Pueraria lobata, sophoradiol saponins, soyasapogenol B saponins, anticomplementary activity, glucuronic acid of saponin
NCBI PubMed ID: 10985074Publication DOI: 10.1055/s-2000-8614Journal NLM ID: 0066751Publisher: George Thieme
Correspondence: Lee H-K
Institutions: Faculty of Pharmaceutical Sciences, Kumamoto University, Kumamoto, Japan, Immunomodulator Research Lab., Korea Research Institute of Bioscience and Biotechnology, Taejeon, South Korea
Methods: biological assays
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14. Compound ID: 28608
|
b-D-Xylp-(1-2)-b-D-Galp-(1-2)-b-D-GlcpA-(1-3)-Subst
Subst = sophoradiol = SMILES C[C@]12CC{3}[C@H](O)C(C)(C)[C@@H]1CC[C@]3(C)[C@@H]2CC=C4[C@@]3(C)CC[C@]5(C)[C@H]4CC(C)(C)C{22}[C@H]5O |
Show graphically |
Structure type: oligomer
; 835 [M+Na]+
Compound class: triterpenoid glycoside
Contained glycoepitopes: IEDB_114701,IEDB_115136,IEDB_136044,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_167188,IEDB_174332,IEDB_190606,IEDB_423153,SB_165,SB_166,SB_187,SB_195,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 11318
Ma CM, Nakamura N, Hattori M "Saponins and C-glycosyl flavones from the seeds of Abrus precatorius" -
Chemical and Pharmaceutical Bulletin 46(6) (1998) 982-987
Two new saponins, 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]hederagenin (named abrus-saponin I) and 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]oleanolic acid 28-beta-D-glucopyranosyI ester (abrus-saponin II), and three new flavones, 6-C-beta-D-glucopyranosyl-4',5-dihydroxy-7,8-dimethoxyflavone (precatorin I), 6-C-[beta-D-apiofuranosyl-(1-->2)-beta-D-glucopyranosyl]-4',5-dihydroxy-7,8-dimethoxyflavone (precatorin II), 6-C-[beta-D-apiofuranosyl-(1-->2)-beta-D-glucopyranosyl]4',5-dihydroxy-7-methoxyflavone (precatorin III), were isolated from the seeds of Abrus precatorius L. together with twelve known compounds including a naturally new saponin, 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]oleanolic acid. Their structures were determined on the basis of chemical and spectroscopic methods, In addition, the unusual NMR spectral behavior of the flavone C-glycosides is also discussed.
saponin, Leguminosae, Abrus precatorius, C-glycosyl flavone
Publication DOI: 10.1248/cpb.46.982Journal NLM ID: 0377775Publisher: Pharmaceutical Society Of Japan
Institutions: Research Institute for Wakan-Yaku, Toyama Medical and Pharmaceutical University, Toyama, Japan
Methods: 13C NMR, 1H NMR, methylation, IR, FAB-MS, acid hydrolysis, UV, extraction, optical rotation measurement, reversed-phase chromatography, HMBC, HMQC, COSY, HOHAHA, API-MS
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15. Compound ID: 28609
|
a-L-Rhap-(1-2)-b-D-Galp-(1-2)-b-D-GlcpA?(%)Me-(1-3)-Subst
Subst = sophoradiol = SMILES C[C@]12CC{3}[C@H](O)C(C)(C)[C@@H]1CC[C@]3(C)[C@@H]2CC=C4[C@@]3(C)CC[C@]5(C)[C@H]4CC(C)(C)C{22}[C@H]5O |
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Structure type: oligomer
; 963 [M+Na]+, 949 [M+Na]+
Trivial name: kaikasaponin III, kaikasaponin III methyl ester
Compound class: triterpenoid glycoside
Contained glycoepitopes: IEDB_115136,IEDB_116887,IEDB_136044,IEDB_136105,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_190606,IEDB_225177,IEDB_423153,IEDB_885823,SB_165,SB_166,SB_187,SB_195,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 11318
Ma CM, Nakamura N, Hattori M "Saponins and C-glycosyl flavones from the seeds of Abrus precatorius" -
Chemical and Pharmaceutical Bulletin 46(6) (1998) 982-987
Two new saponins, 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]hederagenin (named abrus-saponin I) and 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]oleanolic acid 28-beta-D-glucopyranosyI ester (abrus-saponin II), and three new flavones, 6-C-beta-D-glucopyranosyl-4',5-dihydroxy-7,8-dimethoxyflavone (precatorin I), 6-C-[beta-D-apiofuranosyl-(1-->2)-beta-D-glucopyranosyl]-4',5-dihydroxy-7,8-dimethoxyflavone (precatorin II), 6-C-[beta-D-apiofuranosyl-(1-->2)-beta-D-glucopyranosyl]4',5-dihydroxy-7-methoxyflavone (precatorin III), were isolated from the seeds of Abrus precatorius L. together with twelve known compounds including a naturally new saponin, 3-O-[beta-D-glucuronopyranosyl-(1-->2)-beta-D-glucopyranosyl]oleanolic acid. Their structures were determined on the basis of chemical and spectroscopic methods, In addition, the unusual NMR spectral behavior of the flavone C-glycosides is also discussed.
saponin, Leguminosae, Abrus precatorius, C-glycosyl flavone
Publication DOI: 10.1248/cpb.46.982Journal NLM ID: 0377775Publisher: Pharmaceutical Society Of Japan
Institutions: Research Institute for Wakan-Yaku, Toyama Medical and Pharmaceutical University, Toyama, Japan
Methods: 13C NMR, 1H NMR, methylation, IR, FAB-MS, acid hydrolysis, UV, extraction, optical rotation measurement, reversed-phase chromatography, HMBC, HMQC, COSY, HOHAHA, API-MS
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