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TRACE LEVEL ANALYSIS OF REDUCING SUGARS BY HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY (1980)

LAWSON, MARGARET A. ; RUSSELL, GERALD F.

Oxford, UK : Blackwell Publishing Ltd

Journal of food science 45 (1980), S. 0

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ISSN: 1750-3841

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology

Notes: Reducing sugars derivatized with a strong UV chromophore, were detected at nanogram levels using a high-performance liquid chromatograph equipped with an ultra-violet absorbance detector. Sugar standards were derivatized with p-nitrobenzyloxyamine. Quantitative derivatization was. established using thin-layer chromate graphic methods. A μBondapak/Carbohydrate column, with acetonitrile and water as the mobile phase, was used to separate and quantitate 0.5-5.0 ng of individual sugars. Modifications of this method may be developed to detect low-level contamination, adulteration, and decomposition of food constituents.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1365-2621.1980.tb06532.x

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Characterization of Human Plasma Glycoproteins Separated by Two-Dimensional Gel Electrophoresis (1996)

Packer, Nicolle H. ; Wilkins, Marc R. ; Golaz, Olivier ; [et al.]

[s.l.] : Nature Publishing Company

Nature biotechnology 14 (1996), S. 66-70

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ISSN: 1546-1696

Source: Nature Archives 1869 - 2009

Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology

Notes: [Auszug] Purification of protein isoforms for the characterization of post-translational modifications, such as glycosylation, can be laborious and demanding. We report a means of determining monosaccharide composition and the identity of glycoproteins from a single spot on a two-dimensional (2-D) gel. The ...

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1038/nbt0196-66

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A general approach to desalting oligosaccharides released from glycoproteins (1998)

Packer, Nicolle H ; Lawson, Margaret A ; Jardine, Daniel R ; [et al.]

Springer

Glycoconjugate journal 15 (1998), S. 737-747

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ISSN: 1573-4986

Keywords: desalting oligosaccharides ; graphitized carbon ; solid phase ; PNGase F ; electrospray mass spectroscopy ; HPAEC-PAD, high performance anion exchange chromatography with pulsed amperometric ; ESI-MS, electrospray ionization mass spectrometry ; PNGase F ; HexNAc, N-acetyl hexosamine ; Hex, hexose ; GalNAc4S,N-acetylgalactosamine-4-sulfate ; IduA, iduronic acid ; TFA ; SDS, sodium dodecyl sulfate ; NP40, Nonidet P40

Source: Springer Online Journal Archives 1860-2000

Topics: Chemistry and Pharmacology

Notes: Abstract Desalting of sugar samples is essential for the success of many techniques of carbohydrate analysis such as mass spectrometry, capillary electrophoresis, anion exchange chromatography, enzyme degradation and chemical derivatization. All desalting methods which are currently used have limitations: for example, mixed-bed ion-exchange columns risk the loss of charged sugars, precipitation of salt by a non-aqueous solvent can result in co-precipitation of oligosaccharides, and gel chromatography uses highly crosslinked packings in which separation of small oligosaccharides is difficult to achieve. We demonstrate that graphitized carbon as a solid phase extraction cartridge can be used for the purification of oligosaccharides (or their derivatives) from solutions containing one or more of the following contaminants: salts (including salts of hydroxide, acetate, phosphate), monosaccharides, detergents (sodium dodecyl sulfate and Triton X-100), protein (including enzymes) and reagents for the release of oligosaccharides from glycoconjugates (such as hydrazine and sodium borohydride). There is complete recovery of the oligosaccharides from the adsorbent which can also be used to fractionate acidic and neutral glycans. Specific applications such as clean-up of N-linked oligosaccharides after removal by PNGase F and hydrazine, desalting of O-linked glycans after removal by alkali, on-line desalting of HPAEC-separated oligosaccharides and β-eliminated alditols prior to electrospray mass spectrometry, and purification of oligosaccharides from urine are described.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1023/A:1006983125913

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Analyzing glycoproteins separated by two-dimensional gel electrophoresis (1998)

Packer, Nicolle H. ; Lawson, Margaret A. ; Jardine, Daniel R. ; [et al.]

Weinheim : Wiley-Blackwell

Electrophoresis 19 (1998), S. 981-988

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ISSN: 0173-0835

Keywords: Glycoprotein ; Two-dimensional polyacrylamide gel electrophoresis ; α1-Antitrypsin ; α2-HS Glycoprotein ; Protein isoforms ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology

Notes: Two-dimensional (2-D) electrophoresis is the preferred method for separating the glycoforms of proteins. The isoforms usually present as ‘trains’ of spots in the first dimension and may also differ in molecular weight. The primary goal for analyzing the carbohydrate content of glycoprotein spots is to understand the ‘rules’ which govern the migration of glycoproteins in 2-D electrophoresis. These rules can then be used to produce predictive vectors to interpret changes in glycosylation patterns. Techniques for the analysis of oligosaccharides released from glycoproteins which have been electroblotted to PVDF membrane after one-dimensional (1-D) and 2-D preparative gel electrophoresis are described. The oligosaccharides are removed enzymatically (PNGase F of N-linked oligosaccharides) or chemically (β-elimination of O-linked oligosaccharides) and separated by high performance anion exchange chromatography (HPAEC-PAD) and identified by electrospray ionization mass spectrometry (ESI-MS) or analyzed directly by ESI-MS. After enzymic removal of the N-linked oligosaccharides the protein spots can be further analyzed by Edman sequence tagging for identification and quantitation of the protein and by acid hydrolysis for monosaccharide analysis of the O-linked oligosaccharides. These approaches have been proved on 1-D PAGE electroblotted bovine fetuin and human glycophorin A and then used to analyze two abundant proteins which separate as glycoforms on 2-D PAGE preparative narrow range (pH 4.5-5.5) blots of human plasma: α2-HS glycoprotein (human fetuin) and α1-antitrypsin (α1-protease inhibitor). It is apparent that both the macroheterogeneity (site occupation) and microheterogeneity (diversity of structures) of the glycosylation contribute to the separation of protein isoforms in 2-D PAGE.

Additional Material: 9 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/elps.1150190613

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