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  • 1
    Electronic Resource
    Electronic Resource
    Isolation and Characterization of Human Milk Bile Salt-Activated Lipase C-Tail Fragment (1995)
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 10639-10644 
    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/bi00033a039
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  • 2
    Electronic Resource
    Electronic Resource
    Purification and Characterization of N-Acetylglucosamine-6-sulfate Sulfatase from Bovine Kidney: Evidence for the Presence of a Novel Endosulfatase Activity (1994)
    s.l. : American Chemical Society
    Biochemistry 33 (1994), S. 4273-4282 
    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/bi00180a023
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  • 3
    Electronic Resource
    Electronic Resource
    Use of recombinant biotinylated aequorin in microtiter and membrane-based assays: Purification of recombinant apoaequorin from Escherichia coli (1992)
    s.l. : American Chemical Society
    Biochemistry 31 (1992), S. 1433-1442 
    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/bi00120a021
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  • 4
    Electronic Resource
    Electronic Resource
    Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system (1993)
    s.l. : American Chemical Society
    Biochemistry 32 (1993), S. 11087-11099 
    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/bi00092a019
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  • 5
    Electronic Resource
    Electronic Resource
    Protein glycosylation Chaperone mutation in Tn syndrome (2005)
    [s.l.] : Nature Publishing Group
    Nature 437 (2005), S. 1252-1252 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Tn syndrome is a rare autoimmune disease in which subpopulations of blood cells in all lineages carry an incompletely glycosylated membrane glycoprotein, known as the Tn antigen. This truncated antigen has the sugar N-acetylgalactosamine α-linked to either a serine or threonine amino-acid ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/4371252a
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  • 6
    Electronic Resource
    Electronic Resource
    Immobilized Lotus tetragonolobus agglutinin binds oligosaccharides containing the Lex determinant (1997)
    Springer
    Glycoconjugate journal 14 (1997), S. 45-55 
    Details
    ISSN: 1573-4986
    Keywords: fucosylation ; Lotus tetragonolobus agglutinin ; lotus lectin ; affinity chromatography ; Lewis antigens
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A defined set of oligosaccharides and glycopeptides containing α-linked fucose were used to examine the specificity of the immobilized fucose-binding lectin Lotus tetragonolobus agglutinin (LTA1), also known as lotus lectin. Glycans containing the Lewis x determinant (Lex) Galβ1-4[Fucα1-3]GlcNAcβ1-3-R were significantly retarded in elution from high density LTA-Emphaze columns. The lectin also bound the fucosylated lacdiNAc trisaccharide GalNAcβ1-4[Fucα1-3]GlcNAc. The lectin did not bind glycans containing either sialylLex or VIM-2 determinants, nor did it bind the isomeric Lea, Galβ1-3[Fucα1-4]GlcNAc-R. Although 2′-fucosyllactose Fucα1-2Galβ1-4Glc) was retarded in elution from the columns, larger glycans containing the H-antigen Fucα1-2Galβ1-3(4)GlcNAc-R interacted poorly with immobilized LTA. Our results demonstrate that immobilized LTA is effective in isolating glycans containing the Lex antigen and is useful in analyzing specific fucosylation of glycoconjugates. Abbreviations: LTA, Lotus tetragonolobus agglutinin; UEA-1, Ulex europaeus agglutinin-I; LNT, AAL, Aleuria aurantia agglutinin; Galβ1-3GlcNAcβ1-3Galβ1-3Glc; LNnT, Galβ1-4GlcNAcβ1-3Galβ1-3Glc; Lex, Lewis x antigen; Lea, Lewis a antigen; GDPFuc, guanosine 5′-diphosphate-β-L-fucose
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018508914551
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  • 7
    Electronic Resource
    Electronic Resource
    The ruminant parasite Haemonchus contortus expresses an α1,3-fucosyltransferase capable of synthesizing the Lewis x and sialyl Lewis x antigens (1998)
    Springer
    Glycoconjugate journal 15 (1998), S. 789-798 
    Details
    ISSN: 1573-4986
    Keywords: Haemonchus contortus ; α1,3-fucosyltransferase ; Lex antigen ; β1,4-galactosyltransferase ; β1,4-N-acetylgalactosaminyltransferase ; NDV, New Castle Disease ; WFA, Wisteria floribunda agglutinin ; LTA, Lotus tetragonolobus agglutinin ; NEM, N-ethylmaleimide ; Lea, Lewis a antigen ; Lex, Lewis x antigen ; sLex, sialyl Lewis x ; Ley, Lewis y antigen ; SDS-PAGE, sodium dodecyl ; PBS, phosphate buffered saline ; TTBS, Tween-20/Tris buffered saline ; EDTA, ethylenediaminetetraacetic acid ; PMSF, phenylmethylsulfonyl fluoride ; BCA, bicinchoninic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Glycoproteins from the ruminant helminthic parasite Haemonchus contortus react with Lotus tetragonolobus agglutinin and Wisteria floribunda agglutinin, which are plant lectins that recognize α1,3-fucosylated GlcNAc and terminal β-GalNAc residues, respectively. However, parasite glycoconjugates are not reactive with Ricinus communis agglutinin, which binds to terminal β-Gal, and the glycoconjugates lack the Lewis x (Lex) antigen or other related fucose-containing antigens, such as sialylated Lex, Lea, Leb Ley, or H-type 1. Direct assays of parasite extracts demonstrate the presence of an α1,3-fucosyltransferase (α1,3FT) and β1,4-N-acetylgalactosaminyltransferase (β1,4GalNAcT), but not β1,4-galactosyltransferase. The H. contortus α1,3FT can fucosylate GlcNAc residues in both lacto-N-neotetraose (LNnT) Galα1→4GlcNAcβ1→3Galβ1→4Glc to form lacto-N-fucopentaose III Galβ1→ 4[Fucα1→3]GlcNAcβ1→3Galβ1→4Glc, which contains the Lex antigen, and the acceptor lacdiNAc (LDN) GalNAcβ1→4GlcNAc to form GalNAcβ1→4[Fucα1 →3]GlcNAc. The α1,3FT activity towards LNnT is dependent on time, protein, and GDP-Fuc concentration with a Km 50 μ M and a Vmax of 10.8 nmol-mg−1 h−1. The enzyme is unusually resistant to inhibition by the sulfhydryl-modifying reagent N-ethylmaleimide. The α1,3FT acts best with type-2 glycan acceptors (Galβ1→4GlcNAcβ1-R) and can use both sialylated and non-sialylated acceptors. Thus, although in vitro the H. contortus α1,3FT can synthesize the Lex antigen, in vivo the enzyme may instead participate in synthesis of fucosylated LDN or related structures, as found in other helminths.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006912032273
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  • 8
    Electronic Resource
    Electronic Resource
    Secretion of α1,3-galactosyltransferase by cultured cells and presence of enzyme in animal sera (1997)
    Springer
    Glycoconjugate journal 14 (1997), S. 809-819 
    Details
    ISSN: 1573-4986
    Keywords: glycosyltransferase ; enzyme
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Glycosyltransferases are normally synthesized as membrane-anchored proteins. However, we recently found that the murine enzyme UDP-Gal:Galβ1→4GLcNAc (Gal to Gal) α1,3 galactosyltransferase (α1,3GT) is secreted in a soluble form into media by mouse teratocarcinoma F9 cells (Cho SK, Yeh J-C, Cho M, Cummings RD (1996) J Biol Chem 271: 3238–46). To study the biosynthesis of this enzyme and whether secretion of the soluble enzyme is a general phenomenon, a solid-phase assay was developed for the α1,3GT activity. A recombinant and soluble form of the murine α1,3GT was produced in H293 cells (H293-α1,3GT) to aid in optimizing the assay. Desialylated orosomucoid was used as an immobilized acceptor in coated microtiter plates. The formation of product was detected by a biotinylated human-derived anti-α-Gal IgG and streptavidin conjugated to either alkaline phosphatase or the recombinant bioluminescent protein aequorin. Enzyme activity was dependent on the concentrations of asialoorosomucoid, UDP-Gal, α1,3GT and the time of incubation. The assay was also useful in monitoring α1,3GT activity during enzyme enrichment procedures. Using this assay, we found that α1,3GT activity was present in both cell extracts and culture media of several mammalian cell lines. Enzyme activity was also present in the sera from several mammals, but activity was absent in the sera from either humans or baboons. Our results demonstrate the development of a novel assay for the α1,3GT and provide evidence that secretion of the enzyme is a common biological phenomenon. Abbreviations: LNnT, lacto-N-neotetraose (Galβ1→4GlcNAcβ1→3Galβ1→4Glc); PBS/NaN3, phosphate-buffered saline containing sodium azide; α1,3GT, UDP-Gal:Galβ1→4GlcNAc (Gal to Gal) α1,3-galactosyltransferase; BSA, bovine serum albumin; RCA, Ricinus communis agglutinin; SNA, Sambucus nigra agglutinin; RA, all-trans-retinoic acid UDP, uridine diphosphate; ASOSM, asialoorosomucoid; ASF, asailofetuin; ASTransf, asailotransferrin
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018533804015
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  • 9
    Electronic Resource
    Electronic Resource
    The selectin family of carbohydrate-binding proteins: Structure and importance of carbohydrate ligands for cell adhesion (1992)
    New York, NY : Wiley-Blackwell
    BioEssays 14 (1992), S. 849-856 
    Details
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Protein-carbohydrate interactions have been found to be important in many steps in lymphocyte recirculation and inflammatory responses. A family of carbohydrate-binding proteins or lectins, termed selectins, has been discovered and shown to be involved directly in these processes. The three known selectins, termed L-, E- and P-selectins, have domains homologous to other Ca2+-dependent (C-type) lectins. L-selectin is expressed constitutively on lymphocytes, E-selectin is expressed by activated endothelial cells, and P-selectin is expressed by activated platelets and endothelial cells. Here, we review the nature of the carbohydrate determinants in tissues recognized by these selectins. The expression of specific sialylated, fucosylated and sulfated carbohydrates in activated endothelium and high endothelial venules promotes interactions with L-selectin on leukocyte surfaces. In contrast, E- and P-selectins recognize specific carbohydrate determinants related to sialyl Lex antigen on neutrophil and monocyte surfaces. The discovery of the selectins has generated excitemient among glycoconjugate researchers that other carbohydrate-binding proteins and their cognate ligands will be found to function in regulating many types of cellular interactions.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bies.950141210
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