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  • 1
    Electronic Resource
    Electronic Resource
    Major oligosaccharides in the glycoprotein of Friend murine leukemia virus: structure elucidation by one- and two-dimensional proton nuclear magnetic resonance and methylation analysis (1984)
    s.l. : American Chemical Society
    Biochemistry 23 (1984), S. 5628-5637 
    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/bi00318a038
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  • 2
    Electronic Resource
    Electronic Resource
    Carbohydrates of influenza virus. Structure of the oligosaccharides linked to asparagines 406 and 478 in the hemagglutinin of fowl plague virus, strain dutch (1987)
    Springer
    Glycoconjugate journal 4 (1987), S. 17-32 
    Details
    ISSN: 1573-4986
    Keywords: influenza virus ; hemagglutinin ; glycoprotein glycans ; oligosaccharide structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Fowl plague virus, strain Dutch, was metabolically labeled withd-[2-3H]mannose, or withd-[6-3H]glucosamine, and the small subunit (HA2; 0.8 mg in total) of the viral hemagglutinin was isolated by preparative sodium dodecylsulfate-polyacrylamide gel electrophoresis. After proteolytic digestion, the radioactive oligosaccharides were sequentially liberated from the glycopeptides by treatment with different endo-β-N-acetylglucosaminidases and with peptide:N-glycosidase or, finally, by hydrazinolysis. In this manner, four groups of glycans could be obtained by consecutive gel filtrations and were subfractionated by HPLC. The structures of the individual oligosaccharides were analyzed by micromethylation, by acetolysis or by digestion with exoglycosidases. The major species amongst the high mannose glycans at Ans-406 of the viral glycopolypeptide were found to be Manα1-2Manα1-3(Manα1-2Manα1-6)Manα1-6(Manα1-2Manα1-2Manα1-3)Manβ1-4GlcNacβ1-4GlcNAc and Manα1-3(Manα1-2Manα1-6)Manα1-6(Manα1-2Manα1-2Manα1-3)Manβ1-4GlcNAcβ1-4GlcNAc, while the complex glycans at Asn-478 are predominantly GlcNAcβ1-2Manα1-3(GlcNAcβ1-2Manα1-6)Manβ1-4GlcNAcβ1-4GlcNAc (lacking, in part, one of the outerN-acetylglucosamine residues) and GlcNAcβ1-2Manα1-3(Galβ1-4GlcNAcβ1-2Manα1-6)Manβ1-4GlcNAcβ1-4GlcNAc.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01048441
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  • 3
    Electronic Resource
    Electronic Resource
    Glycosylation of glycoprotein 55 encoded by the anaemia-inducing strain of Friend spleen focus-forming virus (1994)
    Springer
    Glycoconjugate journal 11 (1994), S. 133-139 
    Details
    ISSN: 1573-4986
    Keywords: Friend spleen focus-forming virus ; glycoprotein ; oligosaccharide processing ; SFFV
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Normal rat kidney cells, non-productively infected with the anaemia-inducing variant of Friend spleen focus-forming virus (F-SFFVA), were metabolically labelled with [2-3H]mannose. The primary translation product of the viral envelope gene (env), representing a glycoprotein with an apparent molecularM r of 55 000 (gp55), was isolated from cell lysates by immunoaffinity chromatography and purified by preparative SDS/PAGE. Radiolabelled oligosaccharides, released from tryptic glycopeptides by treatment with endo-β-N-acetylglucosaminidase H, were characterized chromatographically, by enzymic digestion and by acetolysis. The results revealed that F-SFFVA gp55 obtained from this source carried predominantly oligomannose type sugar chains with five to nine mannoses. As a characteristic feature, glycans with seven to nine mannoses contained, in part, an additional glucose residue. Although the amount of glucosylated species found was higher in F-SFFVA gp55 (about 25% of total endo-H-sensitive oligosaccharides) than in gp55 of the corresponding polycythaemia-inducing variant (F-SFFVP, 16.3%), the overall glycosylation pattern of the F-SFFVA env product closely resembled that of F-SFFVP gp55 [Strubeet al. (1988)J Biol Chem 263:3762–71]. Hence, our results demonstrate that the different intracellular processing and transport of the primary F-SFFVA env product cannot be attributed to aberrant trimming of its oligomannose type glycans.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731153
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  • 4
    Electronic Resource
    Electronic Resource
    Comparison of the carbohydrate moieties of recombinant soluble Fcε receptor (sFcε RII/sCD23) expressed inSaccharomyces cerevisiae and Chinese hamster ovary cells. Different O-glycosylation sites are used by yeast and mammalian cells (1992)
    Springer
    Glycoconjugate journal 9 (1992), S. 209-216 
    Details
    ISSN: 1573-4986
    Keywords: O-glycosylation in yeast ; O-glycosylation in CHO cells ; soluble FcεRII ; methylation analysis ; sequential degradation with exoglycosidases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Recombinant human soluble low affinity receptor for the Fc portion of IgE (sFcεRII/sCD23) was produced inSaccharomyces cerevisiae or Chinese hamster ovary cells and subjected to carbohydrate analysis. Applied methods included analytical SDS-PAGE, reversed phase HPLC, methylation analysis and sequential degradation with exoglycosidases. The results revealed that sFcεRII derived from Chinese hamster ovary cells is glycosylated exclusively at Ser-147, containing mainly the trisaccharide Sia(α2–3)Gal(β1–3)GalNAc, whereas the yeast derived glycoprotein was glycosylated at Ser-167 and contained only α-mannosyl residues. It is shown here for the first time that different amino acids of a given protein can be O-glycosylated when expressed in yeast or Chinese hamster ovary cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731167
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  • 5
    Electronic Resource
    Electronic Resource
    Structural analysis of neutral glycosphingolipids from Ascaris suum adults (Nematoda: Ascaridida) (1997)
    Springer
    Glycoconjugate journal 14 (1997), S. 389-399 
    Details
    ISSN: 1573-4986
    Keywords: arthro-series glycosphingolipids ; Ascaris suum ; (iso-branched) C17 sphingoid-bases ; neutral glycosphingolipids ; parasitic nematodes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The neutral glycosphingolipid fraction from adults of the pig parasitic nematode, Ascaris suum, was resolved into four components on thin-layer chromatography. The high-performance liquid chromatography-isolated components were structurally analysed by: methylation analysis; exoglycosidase cleavage; gas-liquid chromatography/mass spectrometry; liquid secondary-ion mass spectrometry; and, in particular, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Their chemical structures were determined as: Glc(β1-1)ceramide, Man(β1-4)Glc(β1-1)ceramide, GlcNAc(β1-3)Man(β1-4)Glc(β1-1)ceramide and Gal(α1-3)GalNAc(β1-4)GlcNAc(β1-3)Man(β1-4)Glc(β1-1)ceramide; and were characterized as belonging to the arthro-series of protostomial glycosphingolipids. No glycosphingolipid component corresponding to ceramide tetrasaccharide was detected during these analyses. The ceramide composition of the parent glycosphingolipids was dominated by the 2-(R)-hydroxy C24:0 fatty acid, cerebronic acid, and C17 sphingoid-bases: 15-methylhexadecasphing-4-enine and 15-methylhexadecaphinganine in approximately equal proportions. The component ceramide monohexoside was characterized by an additional 15-methylhexadecaphytosphingosine. Abbreviations: CDH, ceramide dihexoside; Cer, ceramide; CMH, ceramide monohexoside; CPH, ceramide pentahexoside; CTH, ceramide trihexoside; CTetH, ceramide tetrahexoside; Hex, hexose; HexNAc, N-acetylhexosamine; HPTLC, high-performance thin-layer chromatography; LSIMS, liquid secondary-ion mass spectrometry; MALDI-TOF-MS, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry; N-, Nz- and A-glyco(sphingo)lipids, neutral, neutralzwitterionic and acidic glyco(sphingo)lipids, respectively
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018530914067
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  • 6
    Electronic Resource
    Electronic Resource
    Host-cell-specific glycosylation of HIV-2 envelope glycoprotein (1997)
    Springer
    Glycoconjugate journal 14 (1997), S. 785-793 
    Details
    ISSN: 1573-4986
    Keywords: glycoprotein ; glycosylation ; gp120 ; HIV ; MALDI-TOF-MS
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Neutral complex-type N-glycans of the envelope glycoprotein 120 of HIV-2, propagated in different host cells, display cell-type specific variations. In order to identify typical structural elements, glycans were analysed by gel filtration, by enzymic sequencing and, in part, by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The characteristic substituents of di- tri- and tetraantennary carbohydrate units thus observed include N-acetyllactosamine repeats, bisecting N-acetylglucosamine and fucose linked to the chitobiose core as well as to N-acetyllactosamine antennae. Each glycoprotein preparation displayed a characteristic set of glycoforms. Abbreviations: endo H, endo-β-N-acetylglucosaminidase H; E-PHA, Phaseolus vulgaris agglutinin E4; GlcNAcOH, N-acetyl-glucosaminitol; gp120/HUT78(MOLT4/Mφ/PBL/U937), external envelope glycoprotein 120 of HIV-2, strain D194, propagated in HUT78 (MOLT4, Mφ, PBL, U937) cells; gu, glucose units; HPAEC, high-pH anion-exchange chromatography; MALDI-TOF-MS, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry; Mφ, human monocytes/macrophages; PBL, human peripheral blood lymphocytes; PNGase F, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase F
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018577619036
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  • 7
    Electronic Resource
    Electronic Resource
    Glycosylation of the thrombin-like serine protease ancrod fromAgkistrodon rhodostoma venom. Oligosaccharide substitution pattern at eachN-glycosylation site (1993)
    Springer
    Glycoconjugate journal 10 (1993), S. 240-246 
    Details
    ISSN: 1573-4986
    Keywords: glycoprotein ; glycopeptides ; N-linked oligosaccharides ; snake venom
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract In a previous study, we determined the structures of the glycans present in ancrod, a thrombin-like serine protease from the venom of the Malayan pit viperAgkistrodon rhodostoma (Pfeifferet al. (1992)Eur J Biochem 205:961–78). In order to allocate the various carbohydrate chains to distinctN-glycosylation sites of the molecule, we have now isolated individual glycopeptides. Peptide moieties were identified after deglycosylation with peptide-N 4-(N-acetyl-β-glucosaminyl)asparagine amidase F by amino acid analysis and sequencing. Liberated oligosaccharides were assigned to the previously deduced carbohydrate structures by high performance liquid chromatography. Although only quantitative differences were observed, the results indicate that each glycosylation site of ancrod carries its characteristic oligosaccharide pattern. Furthermore, all potential sites were shown to be substituted by carbohydrates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00702206
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  • 8
    Electronic Resource
    Electronic Resource
    Zur polarographischen Reduktion des Rheniums (1950)
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 263 (1950), S. 47-62 
    Details
    ISSN: 0044-2313
    Keywords: Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Die polarographische Reduktion des Rheniums wird in neutralen, alkalischen und sauren Lösungen untersucht. Insgesamt konnten 6 Stromstufen beobachtet werden, die mit Zahlen von 1-6 bezeichnet sind. Die Reduktionspotentiale dieser 6 Stufen, die je nach der Art und Konzentration des Grundelektrolyten Schwankungen unterworfen sind, betragen für die Wellen .Zur Deutung der Wellen wird die Reduktion mit Quecksilber und Zink sowie die Elektrolyse von Kaliumperrhenatlösungen geprüft. In alkalischen, neutralen und sehr schwach sauren Lösungen erhält man die Stufen 1 und 2, entsprechend einem Reduktionsverlauf Bei mittlerer Acidität treten die Stufen 3 und 4 an Stelle von 1 und 2: Die beiden Ionen ReO′4 und Re(VII)Kation stehen miteinander in einem von der Säurekonzentration abhängigen Gleichgewicht. Bei sehr hoher Acidität weisen die Polarogramme 3 Stufen auf und man erhält folgenden Reduktionsverlauf: Analytisch verwertbar sind Stufe 1 aus alkalischer Lösung sowie die Stufen 5 und 6 aus 20 n-Schwefelsäure.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/zaac.19502630107
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  • 9
    Electronic Resource
    Electronic Resource
    Separation of glycoprotein-N-glycans by high-pH anion-exchange chromatography (1990)
    New York, NY : Wiley-Blackwell
    Biomedical Chromatography 4 (1990), S. 193-199 
    Details
    ISSN: 0269-3879
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A series of high-mannose and complex type glycoprotein-N-glycans was subjected to high-pH anion-exchange chromatography. The results revealed that this method represents a useful tool for analytical characterization of single oligosaccharides as well as preparative separation of complex mixtures of carbohydrate side-chains. On the other hand, it became evident that in several cases a combination of different chromatographic techniques is required for efficient separation of individual oligosaccharide species.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bmc.1130040505
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  • 10
    Electronic Resource
    Electronic Resource
    Die elektrolytische und polarographische Reduktion von Molybdänlösungen (1941)
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 246 (1941), S. 258-274 
    Details
    ISSN: 0863-1786
    Keywords: Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: 1. Der Verlauf der elektrolytischen Reduktion von schwefel- und salzsauren Molybdänlösungen wird untersucht. Die Reduktion verläuft über die 5-wertige Stufe bis zum Mo(III). In sehr schwach sauren Lösungen führt sie unmittelbar zu festem Mo(OH)3.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/zaac.19412460303
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