Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Immunochemical properties of oligosaccharide-protein conjugates withKlebsiella-K2 specificity (1979)
    Springer
    Medical microbiology and immunology 165 (1979), S. 271-288 
    Details
    ISSN: 1432-1831
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A series of repeating unit oligomers $$\begin{gathered} \alpha - GlcUA \hfill \\ 1 \downarrow 3 \hfill \\ [ \to 4) - \beta - Man - (1 \to 4) - \alpha - Glc - (1 \to 3) - \beta - Glc - (1 \to ]_n , 1 \leqslant n \leqslant 7 , \hfill \\ \end{gathered} $$ was prepared by depolymerization ofKlebsiella pneumoniae B5055 (01∶K2) capsular polysaccharide (K2-PS) as catalyzed by a bacteriophage-associated glycanase. The monomeric repeating unit [tetrasaccharide, (TS)] and its di- and trimer [octa- and dodecasaccharide (OS and DS)] were conjugated to edestin via reductive aminophenylation and azo coupling at the reducing sugar end group. Rabbit anti-conjugate and anti-bacterial antibodies raised in rabbits were compared with respect to specificity and crossreactivity towards the oligomers of the various molecular sizes, towards parent PS, and towards whole bacteria. Antibodies able to bind specifically to the PS and the bacteria were elicited by all three conjugates. However, the anti-TS conjugate antibodies, in contrast to those obtained with OS and DS conjugate, proved to be practically unable to effect bacterial agglutination. Correspondingly, the TS played an exceptional role in binding to anti-bacterial antibodies. In contrast to the OS and DS it could not fully inhibit precipitation of these antibodies with the bacterial PS. Moreover, the inhibition of the binding of the PS to antibacterial antibodies produced by TS was about 50-fold weaker than that produced by OS, DS, and higher members of the series, all of which were about equally potent inhibitors (on a molar basis). The results show that two repeating units are the minimum requirement for a substantial representation of the PS's serologic specificity. The exceptional behavior of the TS correlates with its lack of theβ-Glc-(1–4)-Man linkage present in all higher members of the series.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02152925
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...