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  • glycoprotein  (3)
  • Springer  (3)
  • 1
    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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  • 2
    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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  • 3
    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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