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  • 1
    Electronic Resource
    Electronic Resource
    Enhanced Binding of Enterotoxigenic Escherichia coli K99 to Amide Derivatives of the Receptor Ganglioside NeuGc-GM3 (1995)
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 1845-1850 
    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/bi00006a004
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  • 2
    Electronic Resource
    Electronic Resource
    Meaning and therapeutic potential of microbial recognition of host glycoconjugates (1998)
    Oxford BSL : Blackwell Science Ltd, UK
    Molecular microbiology 29 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The microbe–host interface is currently in focus because of attempts to develop infection therapy in humans based on either natural receptor saccharide (respiratory and gastrointestinal disease) or sophisticated sialic acid analogues designed from crystal structures (influenza). Most of the known host receptors for microbes are glycoconjugates, and the diversity and selectivity of host tissue glycosylation allow for the tropism of infections. However, among the many binding specificities detected so far, the biological role has been proven only in a few infectious model systems. The existence of multiple specificities of a single microbe is both a complicating factor and a challenge, requiring expanded research with a special demand on glycoscience.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00854.x
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  • 3
    Electronic Resource
    Electronic Resource
    Separation of Sphingosine and Dihydrosphingosine by Reversed Phase Paper Chromatography (1960)
    [s.l.] : Nature Publishing Group
    Nature 188 (1960), S. 312-313 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A crude fraction of sphingolipid long-chain bases was prepared principally according to Carter et al.1. 1-5 mgm. of the bases were transferred to their dinitrophenyl derivatives by keeping them for 30 min. in 4 ml. of a potassium borate buffer, pH. 10, containing 2 µl. fluorodinitrobenzene in ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/188312a0
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  • 4
    Electronic Resource
    Electronic Resource
    Calf small intestine receptors for K99 fimbriated enterotoxeginic Escherichia coli (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 109 (1993), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Non-acid and acid glycolipids were isolated from the small intestine of a newborn calf and tested for the ability to bind Escherichia coli carrying K99 fimbriae. The bacteria did not bind to any of the non-acid glycolipids, whereas in the acid glycolipid fraction several gangliosides were detected which bind to K99 fimbriae. Gangliosides capable of binding K99 fimbriated E. coli were characterized as NeuGc-GM3, NeuGc-GM2, NeuGc-GD1a NeuAc-SPG and NeuAc-SPG. No binding was detected to NeuAc-GM3 and NeuGc-GM1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1993.tb06151.x
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  • 5
    Electronic Resource
    Electronic Resource
    Mouse monoclonal antibody F-3 recognizes the difucosyl type-2 blood group structure (1983)
    Springer
    Immunogenetics 17 (1983), S. 537-541 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00696877
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  • 6
    Electronic Resource
    Electronic Resource
    Lipid pattern and Na+−K+-dependent adenosine triphosphatase activity in the salt gland of duck before and after adaptation to hypertonic saline (1971)
    Springer
    The journal of membrane biology 5 (1971), S. 169-184 
    Details
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Ducks (Anas platyrhynchos) were fed hypertonic saline for eight days, resulting in an activation and hypertrophy of the salt gland. The Na+−K+-dependent adenosine triphosphatase, an enzyme generally assumed to be part of the active Na transport system, increased its specific activity by about 200% during this activation. Sulfatides, the major glycolipids of the salt gland, increased their concentration to the same extent. Cholesterol, cerebrosides, and six phospholipid classes showed an increase of 20–80%.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02107722
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  • 7
    Electronic Resource
    Electronic Resource
    A monoclonal antibody that recognizes both leb and Y (Ley) antigens (1987)
    Springer
    Glycoconjugate journal 4 (1987), S. 399-406 
    Details
    ISSN: 1573-4986
    Keywords: monoclonal antibody ; blood groups ; carbohydrate specificity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A hemagglutinating monoclonal antibody has been obtained from a mouse/mouse hybridoma after immunisation with the leb-active oligosaccharide, lacto-N-difucohexaose I, coupled to edestin. The antibody agglutinated human red cells regardless of Lewis phenotype. Blood group O cells were strongly, agglutinated, and progressively weaker agglutination was observed with A2, B and A2B cells. Blood group A1 and A1B cells were not agglutinated. By examining the binding of the antibody to glycolipids and oligosaccharides it was shown that the Leb and Y (Ley)-haptens bind to a similar extent. Full binding activity was dependent on the presence of, both fucosyl residues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01048373
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  • 8
    Electronic Resource
    Electronic Resource
    Screening for the presence of polyglycosylceramides in various tissues: partial characterization of blood group-active complex glycosphingolipids of rabbit and dog small intestines (1997)
    Springer
    Glycoconjugate journal 14 (1997), S. 231-239 
    Details
    ISSN: 1573-4986
    Keywords: Glycosphingolipids ; polyglycosylceramides ; rabbit ; dog ; small intestine ; blood groups ; helicobacter pylori
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Twenty different human and animal tissues were investigated for the presence of polyglycosylceramides. The glycolipids were isolated by peracetylation of dry tissue residues left after conventional lipid extraction, followed by extraction with chloroform and subsequent Sephadex LH-20, Sephadex LH-60 and silica gel chromatography. In most of the cases only trace amounts of complex glycolipids were found. Distinct bands of glycosphingolipids migrating on TLC plates in a region of brain gangliosides and below were observed in bovine erythrocytes, human leukocytes and human colon mucosa. Definite fractions of polyglycosylceramides were isolated from rabbit small intestine, dog small intestine, human placenta and human leukocytes. The polyglycosylceramides of dog and rabbit intestine were characterized by colorimetric analysis, methylation analysis, mass spectrometry and immunological assays. The dog material contained branched carbohydrate chains with repeated fucosylated N-acetyllactosamine units. Rabbit intestine polyglycosylceramides resembled rabbit erythrocyte polyglycosylceramides with Hex-Hex- terminal determinants but were more complex in respect of sugar composition and structure. The material isolated from dog intestine showed A, H, Lex and Ley blood group activities. Polyglycosylceramides of human erythrocytes, placenta and leukocytes showed strong binding affinity for Helicobacter pylori, while polyglycosylceramide fractions from rabbit and dog intestine were receptor-inactive for this bacterium or displayed only weak and poorly reproducible binding. Abbreviations: C, chloroform; M, methanol; Hex, hexose; HexNAc, N-acetylhexosamine; Fuc, fucose; NeuAc, N-acetylneuraminic acid; NeuGc, N-glycolylneuraminic acid; TLC-thin layer chromatography; FAB/MS, fast atom bombardment mass spectrometry; GC/MS, gas chromatography-mass spectrometry; PGCs, polyglycosylceramides; EI/MS, electron impact ionization mass spectrometry; PBS, phosphate-buffered saline; BSA, bovine serum albumin. The carbohydrate and glycosphingolipid nomenclatures are according to recommendations of IUPAC-IUB Commission on Biochemical Nomenclature (Lipids (1977) 12:455–68; J Biol Chem (1982) 257:3347–51; and J Biol Chem (1987) 262:13–18)
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018545922728
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  • 9
    Electronic Resource
    Electronic Resource
    Selective binding by Helicobacter pylori of leucocyte gangliosides with 3-linked sialic acid, as identified by a new approach of linkage analysis (1998)
    Springer
    Glycoconjugate journal 15 (1998), S. 713-721 
    Details
    ISSN: 1573-4986
    Keywords: Helicobacter pylori ; leucocytes ; glycosphingolipids ; trifluoroacetolysis ; sialic acid ; gas chromatography-mass spectrometry ; linkage position ; NeuAc, N-acetylneuraminic acid ; NeuGc, N-glycolylneuraminic acid ; Gal, galactose ; GlcNAc, N-acetylglucosamine ; GC/MS, gas chromatography mass spectrometry ; DMSO, dimethyl sulphoxide ; ether, diethyl ether ; TFA, trifluoroacetic acid ; TFAA, trifluoroacetic anhydride ; TFAc, trifluoroacetyl ; MALDI-TOF MS, matrix assisted laser desorptionionization time of flight mass spectrometry ; 6-SL, 6-sialyllactose ; 3-SL, 3-sialyllactose ; SPG, sialylparagloboside ; Me, methyl ; FAB MS, fast atom bombardment mass spectrometry ; EI MS, electron ionization mass spectrometry ; DHB, 2,5-dihydroxybenzoic acid ; TLC, thin-layer chromatography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The human gastric pathogen Helicobacter pylori has been shown to bind to glycoconjugates of human leucocytes in a sialic acid-dependent way. In order to improve the identification of the binding epitope, a new technique was developed to analyze the ketosidic linkage position between a terminal sialic acid and the consecutive monosaccharide. Permethylation and reduction with LiAlH4 followed by trifluoroacetolysis in 1000:1 trifluoroacetic anhydride:trifluoroacetic acid (24 h, 100 °C) results in the cleavage of glycosidic but not ketosidic bonds. The disaccharide products were analyzed by gas chromatography-mass spectrometry and sialyl-3 or -6 position and NeuAc or NeuGc are identified by their separate retention times and mass spectra. The method was worked out on model saccharides and applied on five-sugar gangliosides (sialylparaglobosides) of human leucocytes. Radiolabeled Helicobacter pylori was shown to bind to the upper part, but not to the lower part, of the five-sugar interval of a mixture of gangliosides separated on a thin-layer chromatogram. Using a membrane blotting procedure the active and inactive bands were isolated and shown to be NeuAcα2-3- and NeuAcα2-6-paraglobosides, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006992616254
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  • 10
    Electronic Resource
    Electronic Resource
    Recognition of glycoconjugates byHelicobacter pylori: an apparently high-affinity binding of human polyglycosylceramides, a second sialic acid-based specificity (1996)
    Springer
    Glycoconjugate journal 13 (1996), S. 453-460 
    Details
    ISSN: 1573-4986
    Keywords: Helicobacter pylori ; sialic acid ; polyglycosylceramides ; human erythrocytes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Helicobacter pylori has been reported to agglutinate erythrocytes and to bind to various other cells in a sialic acid-dependent way. The binding was inhibited by sialyllactose or fetuin and other sialylated glycoproteins. The specificity apparently requires bacterial growth on agar, since we found that it was lost after growth in the nutrient mixture Ham's F12. Instead, the bacteria bound with high affinity and in a sialic acid-dependent way to polyglycosylceramides of human erythrocytes, a still incompletely characterized group of complex glycolipids. Bacteria grown in F12 medium were metabolically labelled with35S-methionine and analysed for binding to glycolipids on thin-layer chromatograms and to glycoproteins on blots after electrophoresis, with human erythrocyte glycoconjugates in focus. There was no binding to simpler gangliosides including GM3 or sialylparagloboside, or to a mixture of brain gangliosides. In contrast, polyglycosylceramides of human erythrocyte membranes bound at a pmol level. The activity was eliminated by mild acid treatment, mild periodate oxidation or sialidase hydrolysis. Erythrocyte proteins as well as a range of reference glycoproteins did not bind, except band 3, which was weakly active. However, this activity was resistant to periodate oxidation. These results indicate a second and novel sialic acid-recognizing specificity which is expressed independently of the previously described specificity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731478
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