Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_198,SB_44,SB_67,SB_72,SB_86

• Article ID: 9545
  van Kuik JA, Hoffmann RA, Mutsaers JHGM, van Halbeek H, Kamerling JP, Vliegenthart JFG "A 500-MHz 1H-NMR study on the N-linked carbohydrate chain of bromelain. 1H-NMR structural-reporter-groups of Fucose α(1-3)-linked to asparagine-bound N-acetylglucosamine" - Glycoconjugate Journal 3 (1986) 27-34
  

  The 500-MHz 1H-NMR characteristics of the N-linked carbohydrate chain Man-α(1-6)[Xyl-β(1-2)]Man-β(1-4)GlcNAc-β(1-4)[Fuc-α(1-3)]GlcNAc-β1-N-Asn of the proteolytic enzyme bromelain (EC 3.4.22.4) from pineapple stem were determined for the oligosaccharide and the glycopeptide, obtained by hydrazinolysis and Pronase digestion, respectively. The 1H-NMR structural-reporter-groups of the α(1-3)-linked fucose residue form unique sets of data for the alditol as well as for the glycopeptide.

  bromelain, 500-MHz 1H-NMR spectroscopy, N-glycosidic glycan

  Journal NLM ID: 8603310
  Publisher: Kluwer Academic Publishers
  Institutions: Department of Bio-Organic Chemistry, State University of Utrecht, Utrecht, The Netherlands
  Methods: 1H NMR, hydrazinolysis, cation-exchange chromatography
  
   
  
  Ananas comosus
  CSDB ID 127883 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_198,SB_44,SB_67,SB_72,SB_86

• Article ID: 9854
  Takayama S, Isogai A, Tsukamoto C, Shiozawa H, Ueda Y, Hinata K, Okazaki K, Koseki K, Suzuki A "Structures of N-glycosidic saccharide chains in S-glycoproteins, products of S-genes associated with self-incompatibility in Brassica campestris" - Agricultural and Biological Chemistry 53 (1989) 713-722
  

  The N-glycosidic saccharide chains of S-glycoproteins associated with self-incompatibility in Brassica campestris were converted to the pyridylamino derivatives, and their structures were determined with physicochemical data and with the exoglycosidase treatment. These proved to be related to a saccharide chain of pineapple stem bromelain. The three S-glycoproteins, S_8, S_9 and S_<1 2>, carried the common oligosaccharides A and B. This indicates that the specificity of S-glycoproteins was not present in the saccharide chains themselves, but probably in the amino acid sequences.

  Journal NLM ID: 0370452
  WWW link: http://ci.nii.ac.jp/naid/110006324207
  Publisher: Tokyo: Agricultural Chemical Society Of Japan
  Institutions: Faculty of Agriculture, Tohoku University, Japan, Department of Agricultural Chemistry, The University of Tokyo, Tokyo, Japan, Life Science Research Laboratory, Japan Tobacco lnc.
  Methods: gel filtration, 1H NMR, FAB-MS, acid hydrolysis, GC, HPLC, enzymatic digestion
  
   
  
  Brassica campestris
  CSDB ID 101290 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_149158,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_86

• Article ID: 9854
  Takayama S, Isogai A, Tsukamoto C, Shiozawa H, Ueda Y, Hinata K, Okazaki K, Koseki K, Suzuki A "Structures of N-glycosidic saccharide chains in S-glycoproteins, products of S-genes associated with self-incompatibility in Brassica campestris" - Agricultural and Biological Chemistry 53 (1989) 713-722
  

  The N-glycosidic saccharide chains of S-glycoproteins associated with self-incompatibility in Brassica campestris were converted to the pyridylamino derivatives, and their structures were determined with physicochemical data and with the exoglycosidase treatment. These proved to be related to a saccharide chain of pineapple stem bromelain. The three S-glycoproteins, S_8, S_9 and S_<1 2>, carried the common oligosaccharides A and B. This indicates that the specificity of S-glycoproteins was not present in the saccharide chains themselves, but probably in the amino acid sequences.

  Journal NLM ID: 0370452
  WWW link: http://ci.nii.ac.jp/naid/110006324207
  Publisher: Tokyo: Agricultural Chemical Society Of Japan
  Institutions: Faculty of Agriculture, Tohoku University, Japan, Department of Agricultural Chemistry, The University of Tokyo, Tokyo, Japan, Life Science Research Laboratory, Japan Tobacco lnc.
  Methods: gel filtration, 1H NMR, FAB-MS, acid hydrolysis, GC, HPLC, enzymatic digestion
  
   
  
  Brassica campestris
  CSDB ID 101289 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_149158,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_86

• Article ID: 9854
  Takayama S, Isogai A, Tsukamoto C, Shiozawa H, Ueda Y, Hinata K, Okazaki K, Koseki K, Suzuki A "Structures of N-glycosidic saccharide chains in S-glycoproteins, products of S-genes associated with self-incompatibility in Brassica campestris" - Agricultural and Biological Chemistry 53 (1989) 713-722
  

  The N-glycosidic saccharide chains of S-glycoproteins associated with self-incompatibility in Brassica campestris were converted to the pyridylamino derivatives, and their structures were determined with physicochemical data and with the exoglycosidase treatment. These proved to be related to a saccharide chain of pineapple stem bromelain. The three S-glycoproteins, S_8, S_9 and S_<1 2>, carried the common oligosaccharides A and B. This indicates that the specificity of S-glycoproteins was not present in the saccharide chains themselves, but probably in the amino acid sequences.

  Journal NLM ID: 0370452
  WWW link: http://ci.nii.ac.jp/naid/110006324207
  Publisher: Tokyo: Agricultural Chemical Society Of Japan
  Institutions: Faculty of Agriculture, Tohoku University, Japan, Department of Agricultural Chemistry, The University of Tokyo, Tokyo, Japan, Life Science Research Laboratory, Japan Tobacco lnc.
  Methods: gel filtration, 1H NMR, FAB-MS, acid hydrolysis, GC, HPLC, enzymatic digestion
  
   
  
  Brassica campestris
  CSDB ID 101288 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_198,SB_44,SB_67,SB_72,SB_86

• Article ID: 9919
  Bouwstra JB, Spoelstra EC, de Waard P, Leeflang BR, Kamerling JP, Vliegenthart JFG "Conformational studies on the N-linked carbohydrate chain of bromelain" - European Journal of Biochemistry 190 (1990) 113-122
  

  1H- and 13C-NMR assignments for the carbohydrate part of the glycopeptide α-D-Man-(1----6)-[β-D-Xyl-(1----2)]-β-D-Man-(1----4)-β-D- GlcNAc-(1----4)-[α-L-Fuc-(1----3)]-β-D-GlcNAc-(1----N)-Asn approximately, derived from the proteolytic enzyme bromelain (EC 3.4.22.4), have been obtained using homo- and heteronuclear correlation spectroscopy, two-dimensional homonuclear Hartmann-Hahn and nuclear Overhauser enhancement experiments. A conformational model for the carbohydrate chain, deduced from the NMR data and consistent with hard-sphere exo-anomeric calculations shows that the rotamer population about the C-5--C-6 bond of β-Man is restricted to the P omega = 180 rotamer, mainly.

  NCBI PubMed ID: 2364940
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Institutions: Department of Bio-Organic Chemistry, Utrecht University, Utrecht, The Netherlands
  Methods: 13C NMR, 1H NMR, HSEA
  
   
  
  Ananas comosus
  CSDB ID 123438 (all data & tools)
• Article ID: 10449
  Lommerse JPM, Kroon-Batenburg LMJ, Kamerling JP, Vliegenthart JFG "Conformational analysis of the xylose-containing N-glycan of pineapple stem bromelain as part of the intact glycoprotein" - Biochemistry 34 (1995) 8196-8206
  

  The conformational behavior of the N-glycan Man α1-6(Xyl β1-2)Man β1-4GlcNAc β1-4(Fuc α1-3)GlcNAc β of stem bromelain as part of the intact glycoprotein was investigated and compared with that of the same N-glycan as part of a bromelain-derived glycopeptide. Proton chemical shifts of the glycoprotein N-glycan were determined by 2D HOHAHA and 2D NOESY measurements, making use of the glycopeptide 1H NMR data. During each 2D NMR experiment about 4% of the glycoprotein denatured. Experimental data concerning interproton distances of the intact glycoprotein N-glycan were obtained by NOESY 1H NMR spectroscopy. Several theoretical models for the N-glycan, obtained by molecular dynamics simulations of the glycopeptide, were investigated. Comparison of experimental and theoretical NOESY cross peak intensities was performed with the program CROSREL. In comparison with the glycopeptide, the distribution of populations between two main conformations of the Fuc α1-3GlcNAc linkage was altered. In addition, the omega = 60 degrees (gt) rotamer of the Man α1-6Man linkage seems to be present for a significant period of time, whereas in the glycopeptide the omega = -60 degrees (gg) conformation exists exclusively. Except for the Xyl β1-2Man linkage, the mobilities around the glycosidic linkages in the glycoprotein were reduced compared with those in the glycopeptide, especially concerning the Fuc α1-3GlcNAc and Man α1-6Man linkages. These findings might be the result of an interaction of the polypeptide chain with the Fuc α/Man α side of the N-glycan. A qualitative analysis of the NMR spectra showed a larger degree of mobility in the denatured glycoprotein N-glycan than in the intact glycoprotein.

  NCBI PubMed ID: 7794934
  Publication DOI: 10.1021/bi00025a027
  Journal NLM ID: 0370623
  Publisher: American Chemical Society
  Institutions: Department of Bio-Organic Chemistry, Bijvoet Center, Utrecht University, Utrecht, The Netherlands
  Methods: 1H NMR, CD
  
   
  
  Ananas comosus
  CSDB ID 108324 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_149158,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_174333,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_86

• Article ID: 9922
  Sturm A, Bergwerff AA, Vliegenthart JFG "1H-NMR structural determination of the N-linked carbohydrate chains on glycopeptides obtained from the bean lectin phytohemagglutinin" - European Journal of Biochemistry 204 (1992) 313-316
  

  Phytohemagglutinin, the lectin of the common bean Phaseolus vulgaris, is a N-linked glycoprotein with one high-mannose-type and one xylose-containing oligosaccharide side chain per polypeptide. The high-mannose-type glycan is attached to Asn12 and the complex-type glycan to Asn60 [Sturm, A. & Chrispeels, M. J. (1986) Plant Physiol. 81, 320-322]. The structures of the oligosaccharides were elucidated from two glycopeptides obtained from the lectin by Pronase digestion, affinity chromatography on concanavalin-A--Sepharose and gel-filtration chromatography on a column of BioGel P-4. The N-linked glycan structures were investigated by 500-MHz 1H-NMR spectroscopy and were established to be: [formula; see text]

  NCBI PubMed ID: 1740144
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Institutions: Friedrich Miescher-Institute, Basel, Switzerland
  Methods: 1H NMR
  
   
  
  Phaseolus vulgaris
  CSDB ID 123735 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_149158,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_86

• Article ID: 9930
  Priem B, Solokwan J, Wieruszeski JM, Strecker G, Nazih H, Morvan H "Isolation and characterization of free glycans of the oligomannoside type from the extracellular medium of a plant cell suspension" - Glycoconjugate Journal 7 (1990) 121-132
  

  The oligosaccharides Man5GlcNAc and Man3(Xyl)GlcNAc(Fuc)GlcNAc presumed to originate fromN-glycosyl proteins have been purified from an extracellular medium (concentration: 2–5 mg/l of 14 day cultures) of white campion (Silene alba) suspension culture. Their primary structures have been determined by1H-400-MHz NMR spectroscopy and FAB-MS spectrometry. They are probably the result of an autophagic process including protein catabolism due to sucrose starvation. Additional identification of digalactosylglycerol (galactolipid breakdown) argues for this hypothesis.

  oligosaccharide, glycan, glycoconjugate, white campion

  Journal NLM ID: 8603310
  Publisher: Kluwer Academic Publishers
  Institutions: Equipe Polysaccharides Pariétaux des Végétaux, Université des Sciences et Techniques de Lille Flandres-Artois, Villeneuve d'Ascq Cédex, France, Laboratoire de Chimie-Biologique, Université des Sciences et Techniques de Lille Flandres-Artois, Villeneuve d'Ascq Cédex, France
  Methods: gel filtration, 1H NMR, FAB-MS, TLC, GLC, permethylation, PE
  
   
  
  Silene alba
  CSDB ID 128194 (all data & tools)
• Article ID: 10044
  Debray H, Wieruszeski JM, Strecker G "Structural analysis of the carbohydrate chains isolated from mistletoe (Viscum album) lectin I" - Carbohydrate Research 236 (1992) 135-143
  

  Two glycopeptide fractions prepared from mistletoe (Viscum album) lectin I by Pronase digestion were fractioned by affinity chromatography on a concanavalin A-Sepharose column. With 400-MHz 1H NMR spectroscopy, in conjunction with sugar analysis, the following oligosaccharide structures could be determined: two oligomannose-type glycans in the ratio 4:1, one containing six mannose and the other containing five mannose units, both with two 2-acetamido-2-deoxyglucose units. In addition, a mannotriosyl→N,N'-diacetylchitobiose glycan containing a xylosyl group and an α-fucosyl group (1→3)-linked to the 2-acetamido-2-deoxyglycosyl-1 residue, a common core element of many plant glycoproteins, was also observed.

  NCBI PubMed ID: 1291047
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Laboratoire de Chimie Biologique, Unité Mixte de Recherche du CNRS No. 111, Université des Sciences et Techniques de Lille Flandres-Artois, Villeneuve d'Ascq, France
  
   
  
  Viscum album
  CSDB ID 116927 (all data & tools)
• Article ID: 10045
  Wantyghem J, Platzer N, Giner M, Derappe C, Goussault Y "Structural analysis of the carbohydrate chain of glycopeptides isolated from Robinia pseudoacacia seed lectins" - Carbohydrate Research 236 (1992) 181-193
  

  Robinia pseudoacacia seeds contain lectins which are closely related. Pronase digestion of the dimeric and tetrameric lectins, RPA1 and RPA3, gave glycopeptides. The structure of the oligosaccharide was determined by 1H NMR spectroscopy and carbohydrate determination as α-D-Manp-(1→3)-[β-D-Xylp-(1→2)]-[α-D-Manp-(1→6)]-β-D-Manp-(1→4)-β-D-GlcpNAc-(1→4)-[α-L-Fucp-(1→3)]-β-D-GlcpNAc-(1→4)-Asn. It appears that the 34-kDa constitutive polypeptide of RPA1 contains 4-5 carbohydrate chains whereas the 30.5-kDa and 29-kDa subunits of RPA3 contain two and one oligosaccharide chains, respectively.

  NCBI PubMed ID: 1337865
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Unité INSERM 180-UAC CNRS 71, Paris, France
  Methods: 1H NMR
  
   
  
  Robinia pseudoacacia
  CSDB ID 116941 (all data & tools)
• Article ID: 10278
  Gupta D, Arango R, Sharon N, Brewer CF "Differences in the cross-linking activities of native and recombinant Erythrina corallodendron lectin with asialofetuin. Evidence for carbohydrate-carbohydrate interactions in lectin-glycoprotein complexes" - Biochemistry 33 (1994) 2503-2508
  

  A previous study showed that several multivalent galactose-specific lectins including the 14-kDa lectin from calf spleen and the lectins from Erythrina indica, Erythrina cristagalli, and soybean agglutinin formed specific cross-linked complexes with the glycoprotein asialofetuin (ASF) [Mandal, D. K., & Brewer, C. F. (1992) Biochemistry 31, 8465-8472]. In the present study, we have used quantitative precipitation analysis to compare the cross-linking activities of the Gal/GalNAc-specific lectin from Erythrina corallodendron (ECorL) and the recombinant protein (rECorL) which lacks the covalently linked heptasaccharide chains of the native lectin, with ASF. At low concentrations of ASF relative to the lectin, native dimeric ECorL binds to each of the three terminal Gal residues of the three N-linked triantennary chains of ASF and precipitates as a cross-linked complex at a ratio of 1:9 ASF/lectin (monomer). With increasing concentrations of ASF, the 1:9 complex changes to a 1:3 ASF/lectin complex, and at higher ASF concentrations, a 1:1 cross-linked complex forms. However, rECorL, which possesses the same specificity and binding affinity as the native lectin, forms only the 1:9 and 1:3 ASF/lectin complexes. Other Erythrina lectins examined, all of which have covalently attached carbohydrate and are structurally similar to ECorL, show the same cross-linking behavior as native ECorL. On the other hand, the dimeric 14-kDa calf spleen lectin which lacks covalently attached carbohydrate forms only 1:9 and 1:3 cross-linked complexes with ASF [Mandal, D. K., & Brewer, C. F. (1992) Biochemistry 31, 8465-8472].(ABSTRACT TRUNCATED AT 250 WORDS)

  NCBI PubMed ID: 7509639
  Publication DOI: 10.1021/bi00175a020
  Journal NLM ID: 0370623
  Publisher: American Chemical Society
  Institutions: Department of Molecular Pharmacology, Albert Einsten College of Medicine, Bronx, New York 10461
  
   
  
  Erythrina
  CSDB ID 108043 (all data & tools)
• Article ID: 10300
  Shaanan B, Lis H, Sharon N "Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose" - Science 254 (1991) 862-866
  

  The three-dimensional structure of the lactose complex of the Erythrina corallodendron lectin (EcorL), a dimer of N-glycosylated subunits, was determined crystallographically and refined at 2.0 angstrom resolution to an R value of 0.19. The tertiary structure of the subunit is similar to that of other legume lectins, but interference by the bulky N-linked heptasaccharide, which is exceptionally well ordered in the crystal, forces the EcorL dimer into a drastically different quaternary structure. Only the galactose moiety of the lactose ligand resides within the combining site. The galactose moiety is oriented differently from ligands in the mannose-glucose specific legume lectins and is held by hydrophobic interactions with Ala88, Tyr106, Phe131, and Ala218 and by seven hydrogen bonds, four of which are to the conserved Asp89, Asn133, and NH of Gly107. The specificity of legume lectins toward the different C-4 epimers appears to be associated with extensive variations in the outline of the variable parts of the binding sites.

  NCBI PubMed ID: 1948067
  Journal NLM ID: 0404511
  Publisher: Washington, DC: American Association for the Advancement of Science
  Institutions: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892
  
   
  
  Erythrina corallodendron
  CSDB ID 148358 (all data & tools)
• Article ID: 10308
  Fournet B, Leroy Y, Wieruszeski JM, Montreuil J, Poretz RD, Goldberg R "Primary structure of an N-glycosidic carbohydrate unit derived from Sophora japonica lectin" - European Journal of Biochemistry 166 (1987) 321-324
  

  The lectin isolated from Sophora japonica seeds is a glycoprotein which binds oligosaccharides with non-reducing terminal Gal β(1----3/4)GlcNac β1----units. The carbohydrate moiety of the lectin is composed of fucose, xylose, mannose and N-acetylglucosamine. The major glycopeptide of the lectin, prepared by pronase digestion, was derivatized with fluorescein isothiocyanate, purified by PAGE and examined by exoglycosidase digestion as well as purified by gel filtration through Bio-Gel P6-DG and investigated by methylation analysis and 400-MHz 1H-NMR spectroscopy. The primary structure of the glycopeptide was established to be as follows. (Formula: see text). Structures similar to this containing a (β1-2)xylosyl substituent on the core β-mannosyl residue and an inner core (α1-3)fucosyl substituent seem to occur frequently in plant glycoproteins.

  NCBI PubMed ID: 3609011
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Methods: 1H NMR, GC-MS
  
   
  
  Sophora japonica
  CSDB ID 123045 (all data & tools)
• Article ID: 10448
  Tams JW, Welinder KG "Mild chemical deglycosylation of horseradish peroxidase yields a fully active, homogeneous enzyme" - Analytical Biochemistry 228 (1995) 48-55
  

  Horseradish peroxidase isoenzyme C (HRP) contains eight N-linked glycans composed of Man, Xyl, Fuc, and GlcNAc. These glycans were resistant to enzymatic hydrolysis by endoglycosidases peptide-N4-(N-acetyl-β-glucosaminyl) asparagine amidase F, endo-β-N-acetyl-glucosaminidase H, and endo-β-N-acetylglucosaminidase F under conditions where ovalbumin was deglycosylated. However, using anhydrous trifluoromethanesulfonic acid (TFMS) in the presence of 90 mM phenol for 5 min at--10 degrees C, all carbohydrate except GlcNAc was removed. Sixty percent of deglycosylated HRP was active after this TFMS treatment. Benzhydroxamic acid affinity chromatography separated active and inactive deglycosylated HRP. TFMS treatment, however, introduced negative charges in all inactive HRP and in about 90% of the active deglycosylated HRP. The nature of this modification has not been identified. After ion-exchange chromatography, homogeneous and fully active deglycosylated HRP, showing the original pI of 9, electronic absorption spectrum, and enzyme kinetics, was obtained, In this purified product no amino acid modifications were detected by amino acid analysis, partial sequencing, and mass spectrometry of tryptic peptides. The deglycosylated product showed greatly reduced solubility in salt solution compared to that of authentic HRP.

  NCBI PubMed ID: 8572287
  Publication DOI: 10.1006/abio.1995.1313
  Journal NLM ID: 0370535
  Publisher: Academic Press
  Institutions: Department of Protein Chemistry, University of Copenhagen, Denmark
  
   
  
  Armoracia rusticana
  CSDB ID 103157 (all data & tools)
• Article ID: 10687
  Kimura Y, Kusuoku H, Tada M, Takagi S, Funatsu G "Structural analyses of sugar chains from ricin A-chain variant" - Agricultural and Biological Chemistry 54 (1990) 157-162
  

  Two glycopeptides were isolated from a tryptic digest of ricin A-chain variant by gel filtration and reversed-phase HPLC. Their amino acid compositions and sequences showed that Asn-10 and Asn-236 are glycosylated. The sugar chains were liberated from these glycopeptides by hydrazynolysis, N-acetylated, and pyridylaminated. Component analysis and comparison of elution positions of the purified pyridylamino (PA-) sugar chains with those of authentic PA-sugar chains from the major ricin A-chain by reversed-phase HPLC and size fractionation HPLC suggested that both sugar chains linked to Asn-10 and Asn-236 of the ricin A-chain variant are M3FX, identical to that linked to Asn-10 of the major ricin A-chain.

  NCBI PubMed ID: 1368517
  Journal NLM ID: 0370452
  Publisher: Tokyo: Agricultural Chemical Society Of Japan
  Institutions: Laboratory of Biochemistry, Faculty of Agriculture, Okayama University, Japan
  
   
  
  Ricinus communis
  CSDB ID 101317 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_149158,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_86

• Article ID: 10301
  Ashford D, Dwek RA, Welply JK, Amatayakul S, Homans SW, Lis H, Taylor GN, Sharon N, Rademacher TW "The β-1-2-D-xylose and α-1-3-L-fucose substituted N-linked oligosaccharides from Erythrina crista-galli lectin. Isolation, characterization and comparison with other legume lectins" - European Journal of Biochemistry 166 (1987) 311-320
  

  The carbohydrate moieties of Erythrina cristagalli lectin were released as oligosaccharides by hydrazinolysis, followed by N-acetylation and reduction with NaB3H4. Fractionation of the tritium-labelled oligosaccharide mixture by Bio-Gel P-4 column chromatography and high-voltage borate electrophoresis revealed that it is composed of five neutral oligosaccharides. Structural studies by sequential exoglycosidase digestion in combination with methylation analysis and two-dimensional 1H-NMR showed that the major component was the fucose-containing heptasaccharide Man α 3(Man α 6)(Xyl β 2)Man β 4GlcNAc β 4(Fuc α 3)GlcNAcol. This is the first report of such a structure in plant lectins. Small amounts of the corresponding afucosyl hexasaccharide were also identified, as well as three other minor components. The structure of the heptasaccharide shows the twin characteristics of a newly established family of N-linked glycans, found to date only in plants. The characteristics are substitution of the common pentasaccharide core [Man α 3(Man α 6)Man β 4GlcNAc β 4GlcNAc] by a D-xylose residue linked β1----2 to the β-mannosyl residue and an L-fucose residue linked α1----3 to the reducing terminal N-acetylglucosamine residue. The oligosaccharide heterogeneity pattern for Erythrina cristagalli lectin was also found for the lectins from four other Erythrina species and the lectins of two other legumes, Sophora japonica and Lonchocarpus capassa.

  NCBI PubMed ID: 3609010
  Publication DOI: 10.1111/j.1432-1033.1987.tb13516.x
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Institutions: Department of Biochemistry, University of Oxford, Oxford, UK, Department of Biophysics, The Weizmann Institute of Science, Rehovot, Israel
  Methods: gel filtration, 1H NMR, GC-MS, enzymatic digestion, methylation analysis, reduction, PC
  
   
  
  Erythrina corallodendron
  CSDB ID 223040 (all data & tools)
• Article ID: 10685
  Kimura Y, Hase S, Kobayashi Y, Kyogoku Y, Funatsu G, Ikenaka T "Possible pathway for the processing of sugar chains containing xylose in plant glycoproteins deduced on structural analyses of sugar chains from Ricinus communis lectins" - Journal of Biochemistry 101 (1987) 1051-1054
  

  The structures of sugar chains from two lectins in seeds of the castor bean (Ricinus communis) were identified. The sugar chains were liberated from the lectins by hydrazinolysis. After N-acetylation, the reducing-end residues of the sugar chains were coupled with 2-aminopyridine. The pyridylamino derivatives thus obtained were purified by gel filtration and HPLC. The structures of the purified derivatives were identified by component sugar analysis, stepwise exoglycosidase digestion, partial acetolysis, and 500 MHz 1H-NMR spectroscopy. A new processing pathway for sugar chains in plant glycoproteins was proposed on the basis of the structures of the sugar chains.

  NCBI PubMed ID: 3611041
  Journal NLM ID: 0376600
  Publisher: Japanese Biochemical Society
  Institutions: Institute for Protein Research, Osaka University, Japan, Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Japan, Department of Chemistry, Osaka University College of Science, Japan
  Methods: gel filtration, 1H NMR, HPLC, hydrazinolysis
  
   
  
  Ricinus communis
  CSDB ID 232327 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-linked glycopeptide
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_150900,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_198,SB_44,SB_67,SB_72,SB_86

• Article ID: 6546
  Altmann F, Schweiszer S, Weber C "Kinetic comparison of peptide: N-glycosidases F and A reveals several differences in substrate specificity" - Glycoconjugate Journal 12 (1995) 84-93
  

  The initial velocities of hydrolysis of nineteen glycopeptides by peptide: N-glycosidase F and A were determined. Substrates were prepared from bovine fetuin, hen ovalbumin, pineapple stem bromelain, bovine fibrin and taka-amylase. From these glycopeptides, several variants with regard to peptide and carbohydrate structure were prepared and derivatized with dabsyl chloride, dansyl chloride or activated resorufin. Tyrosine containing glycopeptides were also used without an additional chromophore. Enzymatic hydrolysis of glycopeptides was quantified by narrow bore, reversed phase HPLC with turnaround cycle times of down to 6 min, but usually 15 min. KM values ranging from 30 to 64 microM and from 4 to 36 microM were found for N-glycosidase F and A, respectively. Relative velocities of hydrolysis of the different substrates by each enzyme varied considerably. Little, if any, similarity of the performance of N-glycosidase F and A with the different substrates was observed. The minimal carbohydrate structure released by peptide: N-glycosidase F was a di-N-acetylchitobiose. N-glycosidase A could release even a single N-acetylglucosamine, albeit 3000 times slower than a di-N-acetylchitobiose or larger glycans. In general the structure of the intact glycan had little effect on activity, and with both enzymes the rate of hydrolysis appeared to be primarily governed by peptide structure and length. However, N-glycosidase F did not release glycans α-1,3-fucosylated at the asparagine linked N-acetylglucosamine irrespective of the presence of xylose in the substrate.

  NCBI PubMed ID: 7540902
  Journal NLM ID: 8603310
  Publisher: Kluwer Academic Publishers
  Institutions: Institut für Chemie, Univesität fur Bodenkultur Wien, Austria
  
   
  
  Ananas comosus
  CSDB ID 129091 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_150900,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_198,SB_44,SB_67,SB_72,SB_86

• Article ID: 10677
  Lommerse JPM, Kroon-Batenburg LMJ, Kroon J, Kamerling JP, Vliegenthart JFG "Conformations and internal mobility of a glycopeptide derived from bromelain using molecular dynamics simulations and NOESY analysis" - Journal of Biomolecular NMR 6 (1995) 79-94
  

  The conformation and internal flexibility of a glycopeptide Manα1-6 (Xylβ1-2)Manβ1-4GlcNAcβ1-4(Fucα1-3) GlcNAcβ1-N(Asn-Glu-Ser-Ser), prepared from pineapple stem bromelain, have been analyzed using a combination of molecular dynamics (MD) simulations in water with NOESY 1H NMR spectroscopy. Theoretical NOESY cross-peak intensities were calculated by the CROSREL program on the basis of models, obtained from MD simulations, using a full relaxation matrix approach. Special attention was paid to the description of internal flexibility of the hexasaccharide moiety by the use of generalized order parameters, in combination with the application of an individual rotation correlation tme for each monosaccharide residue. The tetrapeptide moiety appeared to be very mobile during the MD simulations, which was confirmed by the absence of NOE cross peaks. For the oligosaccharide part a model was developed to estimate characteristic times for large reorientational motions around the glycosidic linkages, associated with conformational transitions. For the Manα1-6Man and the Fucα1-3GlcNAc linkages such a flexibility was found with a characteristic time of 2 ns. In contrast, the Xylβ1-2Manβ1-4GlcNAcβ1-4GlcNAc part of the glycan appears to be relatively rigid.

  NCBI PubMed ID: 7663144
  Journal NLM ID: 9110829
  Publisher: ESCOM Science Publishers
  Institutions: Department of Bio-Organic Chemistry, Utrecht University, Utrecht, The Netherlands
  Methods: 1H NMR
  
   
  
  Ananas comosus
  CSDB ID 137644 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_115576,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141831,IEDB_142489,IEDB_143632,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153220,IEDB_164174,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_429156,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_77,SB_86

• Article ID: 10699
  Ohtani K, Misaki A "The structure of the glycan moiety of Tora bean (Phaseolus vulgaris) lectin" - Carbohydrate Research 87 (1980) 275-285
  
  Journal NLM ID: 0043535
  Publisher: Elsevier
  
   
  
  Phaseolus vulgaris
  CSDB ID 113495 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: protein
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_115015,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_149135,IEDB_149158,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_86

• Article ID: 10932
  Yoo JY, Ko KS, Seo H-K, Park S, Fanata WID, Harmoko R, Ramasamy NK, Thulasinathan T, Mengiste T, Lim J-M, Lee SY, Lee KO "Limited addition of the 6-arm β1,2-linked N-acetylglucosamine (GlcNAc) residue facilitates the formation of the largest N-glycan in plants" - Journal of Biological Chemistry 290 (2015) 16560-16572
  

  The most abundant N-glycan in plants is the paucimannosidic N-glycan with core β1,2-xylose and α1,3-fucose residues (Man3XylFuc(GlcNAc)2). Here, we report a mechanism in Arabidopsis thaliana that efficiently produces the largest N-glycan in plants. Genetic and biochemical evidence indicates that the addition of the 6-arm β1,2-GlcNAc residue by N-acetylglucosaminyltransferase II (GnTII) is less effective than additions of the core β1,2-xylose and α1,3-fucose residues by XylT, FucTA, and FucTB in Arabidopsis. Furthermore, analysis of gnt2 mutant and 35S:GnTII transgenic plants shows that the addition of the 6-arm non-reducing GlcNAc residue to the common N-glycan acceptor GlcNAcMan3(GlcNAc)2 inhibits additions of the core β1,2-xylose and α1,3-fucose residues. Our findings indicate that plants limit the rate of the addition of the 6-arm GlcNAc residue to the common N-glycan acceptor as a mechanism to facilitate formation of the prevalent N-glycans with Man3XylFuc(GlcNAc)2 and (GlcNAc)2Man3XylFuc(GlcNAc)2 structures.

  glycosyltransferase, glycosylation, plant, post-translational modification (PTM), carbohydrate processing

  Publication DOI: 10.1074/jbc.M115.653162
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: leeko@gnu.ac.kr
  Institutions: Division of Applied Life Science and Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 501 Jinju-daero, Jinju 660-701, Korea, Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907
  Methods: biological assays, MALDI-TOF-MS, genetic manipulations, prediction
  
   
  
  Arabidopsis thaliana
  CSDB ID 61001 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: protein
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_115015,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_149135,IEDB_149158,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_86

• Article ID: 10932
  Yoo JY, Ko KS, Seo H-K, Park S, Fanata WID, Harmoko R, Ramasamy NK, Thulasinathan T, Mengiste T, Lim J-M, Lee SY, Lee KO "Limited addition of the 6-arm β1,2-linked N-acetylglucosamine (GlcNAc) residue facilitates the formation of the largest N-glycan in plants" - Journal of Biological Chemistry 290 (2015) 16560-16572
  

  The most abundant N-glycan in plants is the paucimannosidic N-glycan with core β1,2-xylose and α1,3-fucose residues (Man3XylFuc(GlcNAc)2). Here, we report a mechanism in Arabidopsis thaliana that efficiently produces the largest N-glycan in plants. Genetic and biochemical evidence indicates that the addition of the 6-arm β1,2-GlcNAc residue by N-acetylglucosaminyltransferase II (GnTII) is less effective than additions of the core β1,2-xylose and α1,3-fucose residues by XylT, FucTA, and FucTB in Arabidopsis. Furthermore, analysis of gnt2 mutant and 35S:GnTII transgenic plants shows that the addition of the 6-arm non-reducing GlcNAc residue to the common N-glycan acceptor GlcNAcMan3(GlcNAc)2 inhibits additions of the core β1,2-xylose and α1,3-fucose residues. Our findings indicate that plants limit the rate of the addition of the 6-arm GlcNAc residue to the common N-glycan acceptor as a mechanism to facilitate formation of the prevalent N-glycans with Man3XylFuc(GlcNAc)2 and (GlcNAc)2Man3XylFuc(GlcNAc)2 structures.

  glycosyltransferase, glycosylation, plant, post-translational modification (PTM), carbohydrate processing

  Publication DOI: 10.1074/jbc.M115.653162
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: leeko@gnu.ac.kr
  Institutions: Division of Applied Life Science and Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 501 Jinju-daero, Jinju 660-701, Korea, Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907
  Methods: biological assays, MALDI-TOF-MS, genetic manipulations, prediction
  
   
  
  Arabidopsis thaliana
  CSDB ID 61002 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: protein
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_115015,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_149135,IEDB_149158,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_86

• Article ID: 10932
  Yoo JY, Ko KS, Seo H-K, Park S, Fanata WID, Harmoko R, Ramasamy NK, Thulasinathan T, Mengiste T, Lim J-M, Lee SY, Lee KO "Limited addition of the 6-arm β1,2-linked N-acetylglucosamine (GlcNAc) residue facilitates the formation of the largest N-glycan in plants" - Journal of Biological Chemistry 290 (2015) 16560-16572
  

  The most abundant N-glycan in plants is the paucimannosidic N-glycan with core β1,2-xylose and α1,3-fucose residues (Man3XylFuc(GlcNAc)2). Here, we report a mechanism in Arabidopsis thaliana that efficiently produces the largest N-glycan in plants. Genetic and biochemical evidence indicates that the addition of the 6-arm β1,2-GlcNAc residue by N-acetylglucosaminyltransferase II (GnTII) is less effective than additions of the core β1,2-xylose and α1,3-fucose residues by XylT, FucTA, and FucTB in Arabidopsis. Furthermore, analysis of gnt2 mutant and 35S:GnTII transgenic plants shows that the addition of the 6-arm non-reducing GlcNAc residue to the common N-glycan acceptor GlcNAcMan3(GlcNAc)2 inhibits additions of the core β1,2-xylose and α1,3-fucose residues. Our findings indicate that plants limit the rate of the addition of the 6-arm GlcNAc residue to the common N-glycan acceptor as a mechanism to facilitate formation of the prevalent N-glycans with Man3XylFuc(GlcNAc)2 and (GlcNAc)2Man3XylFuc(GlcNAc)2 structures.

  glycosyltransferase, glycosylation, plant, post-translational modification (PTM), carbohydrate processing

  Publication DOI: 10.1074/jbc.M115.653162
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: leeko@gnu.ac.kr
  Institutions: Division of Applied Life Science and Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 501 Jinju-daero, Jinju 660-701, Korea, Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907
  Methods: biological assays, MALDI-TOF-MS, genetic manipulations, prediction
  
   
  
  Arabidopsis thaliana
  CSDB ID 61003 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: MMXF
Compound class: N-glycan
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_115015,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_1394182,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_149135,IEDB_149158,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_86

• Article ID: 10946
  Strasser R, Bondili JS, Vavra U, Schoberer J, Svoboda B, Glössl J, Léonard R, Stadlmann J, Altmann F, Steinkellner H, Mach L "A unique β1,3-galactosyltransferase is indispensable for the biosynthesis of N-glycans containing Lewis a structures in Arabidopsis thaliana" - Plant Cell 19 (2007) 2278-2292
  

  In plants, the only known outer-chain elongation of complex N-glycans is the formation of Lewis a [Fucα1-4(Galβ1-3)GlcNAc-R] structures. This process involves the sequential attachment of β1,3-galactose and α1,4-fucose residues by β1,3-galactosyltransferase and α1,4-fucosyltransferase. However, the exact mechanism underlying the formation of Lewis a epitopes in plants is poorly understood, largely because one of the involved enzymes, β1,3-galactosyltransferase, has not yet been identified and characterized. Here, we report the identification of an Arabidopsis thaliana β1,3-galactosyltransferase involved in the biosynthesis of the Lewis a epitope using an expression cloning strategy. Overexpression of various candidates led to the identification of a single gene (named GALACTOSYLTRANSFERASE1 [GALT1]) that increased the originally very low Lewis a epitope levels in planta. Recombinant GALT1 protein produced in insect cells was capable of transferring β1,3-linked galactose residues to various N-glycan acceptor substrates, and subsequent treatment of the reaction products with α1,4-fucosyltransferase resulted in the generation of Lewis a structures. Furthermore, transgenic Arabidopsis plants lacking a functional GALT1 mRNA did not show any detectable amounts of Lewis a epitopes on endogenous glycoproteins. Taken together, our results demonstrate that GALT1 is both sufficient and essential for the addition of β1,3-linked galactose residues to N-glycans and thus is required for the biosynthesis of Lewis a structures in Arabidopsis. Moreover, cell biological characterization of a transiently expressed GALT1-fluorescent protein fusion using confocal laser scanning microscopy revealed the exclusive location of GALT1 within the Golgi apparatus, which is in good agreement with the proposed physiological action of the enzyme.

  Publication DOI: 10.1105/tpc.107.052985
  Journal NLM ID: 9208688
  Publisher: Rockville, MD: American Society of Plant Physiologists
  Correspondence: richard.strasser@boku.ac.at
  Institutions: Institute of Applied Genetics and Cell Biology, BOKU, University of Natural Resources and Applied Life Sciences, A-1190 Vienna, Austria, Department of Chemistry, BOKU, University of Natural Resources and Applied Life Sciences, A-1190 Vienna, Austria
  Methods: biological assays, enzymatic digestion, LC-MS, enzymatic assay, genetic manipulations
  
   
  
  Arabidopsis thaliana
  CSDB ID 61058 (all data & tools)