Analyses of N-linked oligosaccharides using a two-dimensional mapping technique

Tomiya, Noboru; Awaya, Juichi; Kurono, Masayasu; Endo, Satoshi; Arata, Yoshiaki; Takahashi, Nobutaka

doi:10.1016/0003-2697(88)90126-1

Cited by 395 publications

(309 citation statements)

References 15 publications

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“…The oligosaccharide fractions were separated on a Bio-Gel P4 column and were reductively aminated with 2-aminopyridine and sodium cyanoborohydride [38]. The pyridylaminated oligosaccharide derivatives were purified by gel filtration on a Sephadex G-15 column followed by two sequential HPLC steps resulting in a single peak of oligosaccharide [28].…”

Section: Preparation Of Pyridylaminated Oligosaccharides From Variousmentioning

confidence: 99%

“…The structures of the pyridylaminated derivatives produced by enzymatic reaction were analyzed by the two-dimensional mapping method as previously described [28]. After each enzymatic reaction, the assay mixture was first subjected to reverse-phase HPLC on a Shim-pack CLC-ODS column (0.6 cm x 15 cm, Shimadzu).…”

Section: Analysis Of the Pyridylaminated Oligosaccharides Produced Bymentioning

confidence: 99%

“…After each enzymatic reaction, the assay mixture was first subjected to reverse-phase HPLC on a Shim-pack CLC-ODS column (0.6 cm x 15 cm, Shimadzu). Each fraction containing oligosaccharide was collected and subjected to a second HPLC, amide-adsorption HPLC on a TSK-GEL Amide-80 column (0.46 cm x 25 cm, Tosoh) and eluted as previously described [28]. Pyridylaminated oligosaccharides were detected in both HPLC systems, by fluorescence using excitation and emission wavelengths of 320 and 400 nm, respectively.…”

Section: Analysis Of the Pyridylaminated Oligosaccharides Produced Bymentioning

confidence: 99%

“…reported a simple and highly sensitive method for assaying GlcNAc transferase 111 in animal cells using pyridylaminated oligosaccharides as acceptor substrates [27]. In the present study, we combined this method with two-dimensional sugar mapping [28] to analyze the substrate specificities of a-1,3-mannosyl-glycoprotein fl-1,2-Nacetylglucosaminyltransferase (GlcNAc transferase I), a-1,6-mannos yl-glycoprotein j-1,2-N-acetylglucosaminyltransferase (GlcNAc transferase II), xylosyl transferase and a-1,3-fucosyl transferase in sycamore cells ( A cerpseudoplutanus L.). From the results of this work, we propose a processing pathway of N-linked oligosaccharides in plant cells.…”

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Studies on synthetic pathway of xylose‐containing N‐linked oligosaccharides deduced from substrate specificities of the processing enzymes in sycamore cells (Acer pseudoplatanus L.)

Tezuka

Hayashi

Ishihara

et al. 1992

European Journal of Biochemistry

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We measured the activities of a-I ,3-mannosyl-glycoprotein ~-l,2-N-acetylglucosaminyltransferase, a-1,6-mannosyl-glycoprotein p-1,2-N-acetylglucosaminyltransferase, ~-3,4-mannosyl-glycoprotein p-1,2-xylosyltransferase and glycoprotein 3-a-~-fucosyltransferase in the Golgi fraction of suspension-cultured cells of sycamore (Acer pseudoplatanus L.) using fluorescence-labelled oligosaccharides as acceptor substrates for these transferase reactions. The structures of the pyridylaminated oligosaccharides produced by these reactions were analyzed by two-dimensional sugar mapping using high-performance liquid chromatography. We demonstrated that The biosynthesis of oligosaccharides in animal cells has been well characterized [l]. This pathway starts from the transfer of Glc3Man9GlcNAc, to nascent polypeptide chains in the endoplasmic reticulum. The processing of Glc3Man9GlcNAcz begins with the removal of three glucose and four mannose residues by sequential reactions of a-glucosidases and aCorrespondence to N . Takahashi, Nagoya City University, College of Nursing, Mizuho-ku, Nagoya, Japan 467.Abbreviations. GlcNAc transferase I, a-I ,3-mannosyl-glycoprotcin ~-1,2-N-acetyIglucosaminyltransferase; GlcNAc transferase 11, a-1,6-mannosyl-glycoprotein ~-1,2-N-acetylglucosaminyltransferase; xylosyl transferase, ~-1,4-mannosyl-glycoprotein B-1,2-xylosyltransferase; fucosyl transferase, glycoprotein 3-a-~-fucosyltransferase; Fuc, fucose; UDP-Xyl, uridine(5')diphospho(l)-/?-xylose; GDP-Fuc, guanosine(5')diphospho-a-L-fucose.Enzymes. a-l,3-Mannosyl-glycoprotein ~-1,2-N-acetylglucosami- mannosidases. The product of these reactions, Man5-GlcNAc,, is the precursor of all N-acetyllactosamine-type oligosaccharides [2]. It is the substrate of GlcNAc transferase I which produces the first N-acetyllactosamine-type intermediate, GlcNAcMan,GlcNAcz. Various N-acetyllactosamine-type oligosaccharides found in animal glycoproteins are produced from GlcNAcMan5GlcNAcz after further modification by a-mannosidase 11, GlcNAc transferase, fucosyl transferase, galactosyl transferase and sialyl transferase. The structures of many oligosaccharides in plant glycoproteins have been elucidated during the last decade [3 -141. These works have revealed that xylose-containing oligosaccharides are widely distributed throughout the plant kingdom, although, xylose-containing N-linked oligosaccharides were also found in glycoproteins from gastropods [15, 161 and Chlorophyceae [17]. The biosynthesis of the oligosaccharide chains in plant glycoproteins has been recently investigatedThe biosynthesis of N-linked oligosaccharide in rice xamylase containing GlcNAc,Man3XylGlcNAcz has been par-

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Section: Preparation Of Pyridylaminated Oligosaccharides From Variousmentioning

confidence: 99%

Section: Analysis Of the Pyridylaminated Oligosaccharides Produced Bymentioning

confidence: 99%

Section: Analysis Of the Pyridylaminated Oligosaccharides Produced Bymentioning

confidence: 99%

mentioning

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Studies on synthetic pathway of xylose‐containing N‐linked oligosaccharides deduced from substrate specificities of the processing enzymes in sycamore cells (Acer pseudoplatanus L.)

Tezuka

Hayashi

Ishihara

et al. 1992

European Journal of Biochemistry

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“…In 1988 (11 years after from the discovery of the Glycoamidase A), she, on the basis of the accumulated oligosaccharide structural data, I published theˆndings of a new analytical technique, namely,``two dimensional (2D)-mapping method,'' along with the structures of 113 neutral examples (11); this method could be used to separate and determine the similarities in the structures of N-linked oligosaccharide moieties of glycoproteins. In 1988, using this new method, my group analyzed samples of urinary and recombinant human erythropoietin (12) and determined the structures of more than 8 types of urinary N-linked oligosaccharides and 13 types of recombinant N-linked oligosaccharides in the human erythropoietin samples.…”

Section: A Introductionmentioning

confidence: 99%

My 30 Years in the Dream of the structural Analyses of the N-linked Oligosaccharides: The Discovery of Glycoamidase A to the Development of the GALAXY Database

Takahashi

2009

TIGG

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Thirty years ago, I discovered a new enzyme, glycoamidase A that cleaves carbohydrate moiety from glycopeptides without aŠecting peptide structures. This brought me to determination that I should commit comprehensive analysis of N-linked oligosaccharide structures in glycoproteins by using this enzyme. Now, the HPLC mapping method developed by myself is a powerful tool to identify the structures of N-glycans. Here I described my 30 years in the dream of the structural analyses of the Nlinked oligosaccharides from the discovery of glycoamidase A to the development of the GALAXY database.

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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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Analyses of N-linked oligosaccharides using a two-dimensional mapping technique

Cited by 395 publications

References 15 publications

Studies on synthetic pathway of xylose‐containing N‐linked oligosaccharides deduced from substrate specificities of the processing enzymes in sycamore cells (Acer pseudoplatanus L.)

Studies on synthetic pathway of xylose‐containing N‐linked oligosaccharides deduced from substrate specificities of the processing enzymes in sycamore cells (Acer pseudoplatanus L.)

My 30 Years in the Dream of the structural Analyses of the N-linked Oligosaccharides: The Discovery of Glycoamidase A to the Development of the GALAXY Database

Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates

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