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  • 1
    Electronic Resource
    Electronic Resource
    Configurations of glycosidic phosphates of lipopolysaccharide from Salmonella minnesota R595 (1982)
    s.l. : American Chemical Society
    Biochemistry 21 (1982), S. 6580-6586 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00268a040
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  • 2
    Electronic Resource
    Electronic Resource
    Lipids and the morphogenesis of Trigonopsis variabilis (1981)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 12 (1981), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1981.tb07627.x
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of Human Plasma Glycoproteins Separated by Two-Dimensional Gel Electrophoresis (1996)
    [s.l.] : Nature Publishing Company
    Nature biotechnology 14 (1996), S. 66-70 
    Details
    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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  • 4
    Electronic Resource
    Electronic Resource
    A general approach to desalting oligosaccharides released from glycoproteins (1998)
    Springer
    Glycoconjugate journal 15 (1998), S. 737-747 
    Details
    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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  • 5
    Electronic Resource
    Electronic Resource
    The elimination ofO-linked glycans from glycoproteins under non-reducing conditions (1994)
    Springer
    Glycoconjugate journal 11 (1994), S. 163-167 
    Details
    ISSN: 1573-4986
    Keywords: O-linked sugars ; mucin ; glycoprotein ; β-elimination ; sugar hydrazones ; reducing sugars
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A simple procedure is described for the elimination ofO-linked glycans from bovine submaxillary mucin under non-reducing conditions, using triethylamine in aqueous hydrazine. The glycans were isolated as the hydrazones, which were converted to the reducing glycans by exchange with acetone in neutral aqueous solution. The glycan alditols obtained after reduction corresponded to those obtained by the reductive β-elimination ofO-glycans.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731156
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  • 6
    Electronic Resource
    Electronic Resource
    Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation (1994)
    Springer
    Glycoconjugate journal 11 (1994), S. 180-186 
    Details
    ISSN: 1573-4986
    Keywords: N-terminal sequencing ; glycoprotein ; glycan analysis ; covalent immobilization ; mass spectrometry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered. In the case of heavily glycosylated domains such as theO-glycosylated mucins, which have no available protease sites, this approach is not possible. Here we introduce a new method to gain site-specific compositional data on the oligosaccharides attached to a single amino acid. Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection. The PTH-Asn(Sac) derivative was further characterized by ionspray mass spectrometry. Comparison between an endoproteinase Glu-C glycopeptide and a tryptic glycopeptide showed that the oligosaccharide attached to Asn494 was stable after at least 10 cycles of Edman degradation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731216
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  • 7
    Electronic Resource
    Electronic Resource
    Glycobiology and proteomics: Is mass spectrometry the holy grail? (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 1872-1882 
    Details
    ISSN: 0173-0835
    Keywords: Glycoprotein ; Mass spectrometry ; Two-dimensional polyacrylamide gel electrophoresis ; Proteome ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: One characteristic of glycoproteins is that they are separated by two-dimensional electrophoresis (2-D PAGE) into typical ‘trains’ of protein spots which separate on the basis of different isoelectric point (pI) and/or molecular mass. The pattern of these trains often varies in development and disease. While the isoforms differ both in the number of sites of glycosylation and the types of carbohydrate attached to the protein, classical methods of glycan analysis are insensitive at the levels typically separated by 2-D PAGE. Developments in mass spectrometry technologies have enabled the characterization of most of the oligosaccharide attributes to be determined on picomole amounts of protein. These techniques are beginning to allow the glycoform heterogeneity on 2-D separated glycoproteins to be analyzed.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191105
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  • 8
    Electronic Resource
    Electronic Resource
    Analyzing glycoproteins separated by two-dimensional gel electrophoresis (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 981-988 
    Details
    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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  • 9
    Electronic Resource
    Electronic Resource
    Proteome analysis of glycoforms: A review of strategies for the microcharacterisation of glycoproteins separated by two-dimensional polyacrylamide gel electrophoresis (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 452-460 
    Details
    ISSN: 0173-0835
    Keywords: Proteome ; Glycoprotein ; Two-dimensional polyacrylamide gel electrophoresis ; Post-translational modifications ; Oligosaccharides ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Preparative two-dimensional polyacrylamide electrophoresis (2-D PAGE) is a method of separation which for the first time allows protein isoforms to be readily purified for subsequent analysis. The profile of the 2-D separation of the protein complement (proteome) of eukaryotic cells and tissues typically contains obvious ‘trains’ of spots which differ in pI and/or apparent molecular mass. These are usually isoforms of the same protein and result from post-translational modifications. There is growing evidence that alterations to the glycosylation and/or phosphorylation of a protein can be correlated with developmental and pathological changes; these changes can be visualised on the 2-D separation. It is not clear, however, how these modifications alter the structural properties of the protein and affect their migration in this mode of separation. Strategies need to be developed to obtain a more detailed understanding of the reason for the appearance of isoforms as discrete spots on 2-D PAGE. Standard proteins, fetuin and ovalbumin, were used to monitor the effect of the removal of glycans and phosphates on the migration of the glycoproteins in the 2-D system. The isoforms were not simply explained by the presence or absence of a single modification. To further investigate the reasons for the different migration of the isoforms it is necessary to characterise the modifications in more detail. Unlike protein analysis, until recently the available methodology for the analysis of the glycans attached to proteins has not been sensitive enough to allow analysis of single spots in gels or blots resulting from 2-D electrophoresis. In this paper we review current and future strategies for characterisation of protein modifications using single spots from 2-D gels.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180320
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  • 10
    Electronic Resource
    Electronic Resource
    The Dictyostelium discoideum proteome - the SWISS-2DPAGE database of the multicellular aggregate (slug) (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 491-497 
    Details
    ISSN: 0173-0835
    Keywords: Dictyostelium discoideum ; Two-dimensional polyacrylamide gel electrophoresis ; Proteome ; Amino acid analysis ; Isoelectric point ; Molecular weight ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The cellular slime mold Dictyostelium discoideum is a eukaryotic microorganism which has developmental life stages attractive to the cell and molecular biologist. By displaying the two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) protein map of different developmental stages, the key molecules can be identified and characterised, allowing a detailed understanding of the D. discoideum proteome. Here we describe the preparation of reference gel of the D. discoideum multicellular aggregate, the slug. Proteins were separated by 2-D PAGE with immobilised pH gradients (pH 3.5-10) in the first dimension and sodium dodecyl sulfate (SDS)-PAGE in the second dimension. Micropreparative gels were electroblotted onto polyvinylidene difluoride (PVDF) membranes and 150 spots were visualised by amido black staining. Protein spots were excised and 31 were putatively identified by matching their amino acid composition, estimated isoelectric point (pI) and molecular weight (Mr) against the SWISS-PROT database with the ExPASy AAcompID tool (http://expasy.hcuge.ch/ch2d/aacompi.html). A total of 25 proteins were identified by matching against database entries for D. discoideum, and another six by crossspecies matching against database entries for Saccharomyces cerevisiae proteins. This map will be available in the SWISS-2DPAGE database.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180325
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