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  • 1
    Electronic Resource
    Electronic Resource
    Chemoenzymatic galactosialylation with integrated cofactor regeneration (1993)
    Springer
    Glycoconjugate journal 10 (1993), S. 26-33 
    Details
    ISSN: 1573-4986
    Keywords: N-Acetylneuraminic acid ; galactosyltransferase ; α(2-6)sialyltransferase ; cofactor regeneration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract As a precursor for the chemical synthesis of sialylated oligosaccharides, the trisaccharide glycoside Neu5Ac α(2-8)Galβ(1-4)GlcNAcβ(1-O)-pent-4-ene was synthesized starting from GlcNAcβ(1-O)-pent-4-ene, UDP-glucose andN-acetylneuraminic acid in a one pot reaction employing galactosyltransferase and α(2-6)sialyl-transferase in a complete cofactor regeneration system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731183
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  • 2
    Electronic Resource
    Electronic Resource
    Hydrolase-catalyzed β-mannosylations (1998)
    Springer
    Glycoconjugate journal 15 (1998), S. 757-767 
    Details
    ISSN: 1573-4986
    Keywords: β-mannosidase ; β-galactosidase ; β-mannosylation ; transfer mechanism ; cosolvent ; immobilization ; DMF, dimethyl formamide ; DMSO, dimethyl sulfoxide ; Glyp, glycopyranosyl ; GlypOMe, methyl glycopyranoside ; GlypOpNP, 4-nitrophenyl glycopyranoside ; TMS, tetramethyl silane ; ax, axial ; eq
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Transmannosylations catalysed by β-mannosidase from snail viscera or β-galactosidase from Aspergillus oryzae were accomplished with 4-nitrophenyl β D -mannopyranoside as donor substrate. With suitable hydrophobic acceptor molecules preferentially β1-4-linked disaccharides were obtained. The activities of both glycosidases in buffer cosolvent mixtures were determined, and conditions for their immobilization were elaborated and optimized. A model of the enzymic transfer mechanism is suggested.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006999614526
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  • 3
    Electronic Resource
    Electronic Resource
    In vitro α1-3 or α1-4 fucosylation of type I and II oligosaccharides with secreted forms of recombinant human fucosyltransferases III and VI (1998)
    Springer
    Glycoconjugate journal 15 (1998), S. 873-883 
    Details
    ISSN: 1573-4986
    Keywords: Fucosyltransferase ; Lewis oligosaccharides ; mass spectrometry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Transgalactosylation of chitobiose and chitotriose employing β-galactosidase from bovine testes yielded mixtures with β1-3 linked galactose (type I) and β1-4 linked galactose (type II) in a final ratio of 1:1 for the tri- and 1:1.4 for the tetrasaccharide. After 24 h incubations of the two purified oligosaccharide mixtures with large amounts (20-fold increase compared with standard conditions) of human α1, 3/4-fucosyltransferase III (FucT III), the type I tri-/tetrasaccharides were completely converted to the Lewisa structure, whereas approximately 10% fucosylation of the type II isomers to the Lewisx oligosaccharides was observed in long-term incubations. Employing large amounts of human α1, 3-fucosyltransferase VI (FucT VI), the type I trisaccharide substrate was exclusively fucosylated at the proximal O-4 substituted N-acetylglucosamine (GlcNAc) (20%) whereas almost all of the type II isomers was converted to the corresponding Lewisx product. 45% of the type I tetrasaccharide was fucosylated at the second GlcNAc solely by FucT VI. The type II isomer was almost completely α1-3 fucosylated to yield the Lewisx derivative with traces of a structure that contained an additional fucose at the reducing GlcNAc. The results obtained in the present study employing high amounts of enzyme confirmed our previous results that FucT III acts preponderantly as a α1-4 fucosyltransferase onto GlcNAc in vitro. Human FucT VI attaches fucose exclusively in an α1-3 linkage to 4-substituted GlcNAc in vitro and does not modify any 3-substituted GlcNAc to yield Lewisa oligosaccharides. With 8-methoxycarbonyloctyl glycoside acceptors used under standard conditions, FucT III acts exclusively on the type I and FucT VI only on the type II derivative. With lacto-N-tetraose, lacto-N-fucopentraose I, or LS-tetrasaccharide as substrates, FucT III modified the 3-substituted GlcNAc and the reducing glucose; FucT VI recognized only lacto-N-neotetraose as a substrate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006907031940
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  • 4
    Electronic Resource
    Electronic Resource
    Synthesis of polyterephthalates derived from dianhydrohexitols (1984)
    Springer
    Polymer bulletin 11 (1984), S. 365-369 
    Details
    ISSN: 1436-2449
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Summary By melting condensation of terephthalic acid dichloride and 1,4∶3,6-dianhydrohexitols as well as selectively prepared lower oligomers thereof the formation of polyterephthalates is achieved. These polyesters are characterized by 1H-NMR spectra vapour pressure osmometry (VPO), differential scanning calorimetry (DSC), viscosity measurements and combustion analyses. Their preparation and properties are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00254275
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  • 5
    Electronic Resource
    Electronic Resource
    Simple and non-radioactive method for determination of sialyltransferase activity (1997)
    Springer
    Biotechnology techniques 11 (1997), S. 323-326 
    Details
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A new, non-radioactive and cheap colorimetric method for determination of activity of sialyltransferases of various specifities using natural substrates based on 2-thiobarbituric acid assay is presented. The assay was tested with three different sialyltransferases (a-2,3 and a-2,6) and compared with the radioactive assay.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018423513138
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  • 6
    Electronic Resource
    Electronic Resource
    Vorteilhafte Verwendung einfachen Kieselgels (〈 63 μ) in der präparativen Hochdruck-Flüssigkeits-Chromatographie (HPLC) (1980)
    Springer
    Fresenius' Zeitschrift für analytische Chemie 304 (1980), S. 369-373 
    Details
    ISSN: 1618-2650
    Keywords: Chromatographie, HPLC ; Untersuchung verschiedener Kieselgele, Disaccharidderivate als Beispiel
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Zusammenfassung Es wird über die Berechnung sowie die Konstruktion eines aufeinander abgestimmten Systems aus Trennsäulen und Füllgefäß berichtet. Die HPLC-Anlage und der Füllvorgang werden beschrieben. Vergleichende Aufnahmen der van Deemter-Kurven zwischen dem preiswerten Kieselgel K3 (〈 63 μ) und den eng geschnittenen Kieselgelen K1 (15–25 μ) sowie K2 (25–40 μ) werden vorgenommen. Danach erweist sich Kieselgel K3 als besonders vorteilhaft für den Einsatz in der präparativen HPLC, was an einem Beispiel exemplarisch mit der Trennung isomerer Disaccharid-Derivate gezeigt wird.
    Notes: Summary The calculation and construction of an adjusted system of columns and filling vessel is reported. The HPLC device and the filling process are described. Comparative studies between the van Deemter graphs of the low-costing silica gel K3 (〈 63 μ) and silica gels of defined particle size (K1: 15–25 μ und K2 25–40 μ) are performed. The results prove that silica gel K3 is advantageously applied in preparative HPLC. This is demonstrated with the efficient separation of isomeric disaccharide derivatives as an example.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00480606
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