Reducing-End Modification of N-Linked Oligosaccharides with Tyrosine

Tamura, Toshiaki; Wadhwa, Manpreet S.; Rice, Kevin G.

doi:10.1006/abio.1994.1050

Cited by 54 publications

(34 citation statements)

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“…7). The 500-MHz NMR spectra of the oligosaccharide product revealed characteristic anomeric proton and N-acetyl signals for GlcNAc 1, 2, 5, and 5Ј as well as the Boc tyrosine group (18) sessed the xylose linked to the 2-position of ␤-linked mannose (17). On this basis, the oligosaccharide product was assigned to that of structure 12 of Fig.…”

Section: Figmentioning

confidence: 93%

“…Tyrosinamide biantennary oligosaccharides, with or without a core fucose, were prepared from bovine fetuin and porcine fibrinogen as described previously (18,19). A biantennary oligosaccharide (Fig.…”

mentioning

confidence: 99%

“…The overall yield was about 30%. The identity of each oligosaccharide product was established by NMR and electrospray mass spectrometry as described previously (18,19).…”

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confidence: 99%

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Purification and Specificity of β1,2-Xylosyltransferase, an Enzyme That Contributes to the Allergenicity of Some Plant Proteins

Zeng

Bannon

Thomas

et al. 1997

Journal of Biological Chemistry

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Section: Figmentioning

confidence: 93%

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confidence: 99%

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Purification and Specificity of β1,2-Xylosyltransferase, an Enzyme That Contributes to the Allergenicity of Some Plant Proteins

Zeng

Bannon

Thomas

et al. 1997

Journal of Biological Chemistry

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“…1) were prepared from bovine fetuin as described previously (21,22). Man 9 GlcNAc 2 -N-tert-butoxycarbonyl-L-tyrosine was prepared from soybean agglutinin (23), Bis 2 from ovotransferrin (24), and Fuc-Tri and Tetra from human orosomucoid (25).…”

Section: Methodsmentioning

confidence: 99%

“…The reducing ends were converted into glycosylamines and then derivatized with N-tert-butoxycarbonyl-L-tyrosine N-hydroxysuccinimide ester (Sigma). The tyrosinylated oligosaccharides were purified by RP-HPLC, and the structures were characterized by 1 H NMR and fast atom bombardment mass spectrometry (21)(22)(23)(24)(25)(26)(27).…”

Section: Methodsmentioning

confidence: 99%

Xanthosoma sagittifolium Tubers Contain a Lectin with Two Different Types of Carbohydrate-binding Sites

Mo¹,

Rice²,

Evers³

et al. 1999

Journal of Biological Chemistry

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An unusual lectin possessing two distinctly different types of carbohydrate-combining sites was purified from tubers of Xanthosoma sagittifolium L. by consecutive passage through two affinity columns, i.e. asialofetuin-Sepharose and invertase-Sepharose. SDS-polyacrylamide gel electrophoresis, N-terminal amino acid sequencing, and gel filtration chromatography of the purified lectin showed that the X. sagittifolium lectin is a heterotetrameric protein composed of four 12-kDa subunits (␣ 2 ␤ 2 ) linked by noncovalent bonds. The results obtained by quantitative precipitation and hapten inhibition assays revealed that the lectin has two different types of carbohydrate-combining sites: one type for oligomannoses, which preferentially binds to a cluster of nonreducing terminal ␣1,3-linked mannosyl residues, and the other type for complex N-linked carbohydrates, which best accommodates a non-sialylated, triantennary oligosaccharide with N-acetyllactosamine (i.e. Gal␤1,4GlcNAc-) or lacto-N-biose (i.e. Gal␤1,3GlcNAc-) groups at its three nonreducing termini.Lectins are (glyco)proteins of nonimmune origin that agglutinate cells and/or precipitate complex carbohydrates (1). It is their unique ability to recognize and bind reversibly to specific carbohydrate ligands without chemically modifying them that distinguishes lectins from other carbohydrate-binding proteins and enzymes and that makes lectins invaluable tools in biomedical and glycoconjugate research.Lectins are ubiquitous in the biosphere. In the plant kingdom, they are traditionally found in the dicotyledons, especially in seeds (2-4). However, during the last decade, lectins from monocotyledonous families such as Alliaceae (5-7), Amaryllidaceae (8 -10), Araceae (11-14), Liliaceae (15, 16), and Orchidaceae (17) have been isolated and characterized. Interestingly, they all belong to a single monocot mannose-binding lectin superfamily with respect to their molecular structures, sequence homologies, and exclusive specificity for D-mannose (18).Recently, Van Damme et al. (11) described the isolation of lectins from several Araceae species, viz. Arum maculatum, Colocasia esculenta, Xanthosoma sagittifolium, and Dieffenbachia sequina. Based on their molecular structure, taxonomic relationship, and high sequence homology to the aforementioned mannose-binding lectins, they clearly belong to the monocot mannose-binding lectin superfamily. However, compared with the other members of the superfamily, these lectins exhibit either very weak or no affinity for D-mannose, whereas they bind with great avidity to asialoglycoproteins. Therefore, a detailed investigation of their carbohydrate-binding specificities has been undertaken. The results presented in this study reveal that one of these lectins, i.e. the lectin from X. sagittifolium (XSL), 1 possesses two distinctly different types of binding sites: one type for oligomannoses and the other for complex carbohydrates, which best accommodates an asialo triantennary N-linked glycan. The knowledge obtained from this study might ...

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Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates

Harvey¹

1999

Mass Spectrom. Rev.

693

249

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This review describes the application of matrix‐assisted laser desorption/ionization (MALDI) mass spectrometry to carbohydrate analysis and covers the period 1991–1998. The technique is particularly valuable for carbohydrates because it enables underivatised, as well as derivatised compounds to be examined. The various MALDI matrices that have been used for carbohydrate analysis are described, and the use of derivatization for improving mass spectral detection limits is also discussed. Methods for sample preparation and for extracting carbohydrates from biological media prior to mass spectrometric analysis are compared with emphasis on highly sensitive mass spectrometric methods. Quantitative aspects of MALDI are covered with respect to the relationship between signal strength and both mass and compound structure. The value of mass measurements by MALDI to provide a carbohydrate composition is stressed, together with the ability of the technique to provide fragmentation spectra. The use of in‐source and post‐source decay and collision‐induced fragmentation in this context is described with emphasis on ions that provide information on the linkage and branching patterns of carbohydrates. The use of MALDI mass spectrometry, linked with exoglycosidase sequencing, is described for N‐linked glycans derived from glycoproteins, and methods for the analysis of O‐linked glycans are also covered. The review ends with a description of various applications of the technique to carbohydrates found as constituents of glycoproteins, bacterial glycolipids, sphingolipids, and glycolipid anchors. © 1999 John Wiley & Sons, Inc., Mass Spec Rev 18: 349–451, 1999

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Reducing-End Modification of N-Linked Oligosaccharides with Tyrosine

Cited by 54 publications

References 0 publications

Purification and Specificity of β1,2-Xylosyltransferase, an Enzyme That Contributes to the Allergenicity of Some Plant Proteins

Purification and Specificity of β1,2-Xylosyltransferase, an Enzyme That Contributes to the Allergenicity of Some Plant Proteins

Xanthosoma sagittifolium Tubers Contain a Lectin with Two Different Types of Carbohydrate-binding Sites

Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates

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