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  • 1
    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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  • 2
    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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  • 3
    Electronic Resource
    Electronic Resource
    Recognition of glycoconjugates by Helicobacter pylori. Comparison of two sialic acid-dependent specificities based on haemagglutination and binding to human erythrocyte glycoconjugates (1997)
    Springer
    Glycoconjugate journal 14 (1997), S. 467-471 
    Details
    ISSN: 1573-4986
    Keywords: Helicobacter pylori ; human erythrocytes ; sialic acid ; polyglycosylceramides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Helicobacter pylori expresses separate binding characteristics depending on growth conditions, as documented by binding to human erythrocyte glycoconjugates. Cells grown in Ham's F12 liquid medium exhibited a selective sialic acid-dependent binding to polyglycosylceramides, PGCs (Miller-Podraza et al. (1996) Glycoconjugate J 13:453–60). There was no binding to traditional sialylated glycoconjugates like shorter-chain gangliosides, glycophorin or fetuin. However, cells grown on Brucella agar bound both to PGCs and other sialylated glycoconjugates. Fetuin was an effective inhibitor of haemagglutination caused by agar-grown cells, but had no or a very weak inhibitory effect on haemagglutination by F12-grown bacteria. PGCs were strong inhibitors in both cases, while asialofetuin was completely ineffective. The results indicate that H. pylori is able to express two separate sialic acid-dependent specificities, one represented by binding to fetuin, as described before, and another represented by a selective binding to PGCs. Abbreviations: PGCs, polyglycosylceramides; TLC, thin-layer chromatography; SDS PAGE, sodium dodecylsulfate polyacrylamide gel electrophoresis; BSA, bovine serum albumin; C, chloroform; M, methanol. 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:1018599401772
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  • 4
    Electronic Resource
    Electronic Resource
    Selected ion monitoring of glycosphingolipid mixtures. Identification of several blood group type glycolipids in the small intestine of an individual rabbitThe results in this communication were reported at the 11th FEBS Meeting, Copenhagen, Denmark (1977). (1979)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 6 (1979), S. 231-241 
    Details
    ISSN: 0306-042X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A novel application of selected ion monitoring was used for a mixture of non-acid glycosphingolipids of one rabbit small intestine. Earlier studies of permethylated and permethylated-reduced (LiAlH4) derivatives of model compounds have revealed a specificity and abundance of saccharide ions (terminal monosaccharide(s), disaccharide, trisaccharide, etc., and all sugars plus fatty acid) and of ceramide fragments that permit a conclusive detection of separate glycolipid species in a mixture. The sample (50-200 μg) was evaporated slowly (1-5°C min-1 form 150-350°C) from the direct inlet probe of an MS 902 mass spectrometer (electron ionization). Mass spectra with fragments up to about m/z 2000 were collected on-line by a computer system. A successive partial separation was obtained for glycolipids with from one up to seven sugars. The structures of eight different compounds were identified. They all had 16:0, 22:0 and 24:0 2-hydroxy fatty acids and 18:0 trihydroxy base (phytosphingosine) as major ceramide components. The dominating complex glycolipid was a hexaglycosylceramide with a blood group B type of sequence. A blood group A type sequence was found in a second hexaglycosylceramide. In support of this, the native mixture showed blood group A and B activity. An intense peak, m/z 182, collected from methylated derivatives was evidence for a dominating type 2 carbohydrate chain of the core tetrasaccharide.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200060603
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  • 5
    Electronic Resource
    Electronic Resource
    Identification of two-dimensional gel electrophoresis resolved yeast proteins by matrix-assisted laser desorption ionization mass spectrometry (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 418-423 
    Details
    ISSN: 0173-0835
    Keywords: Yeast ; Two-dimensional polyacrylamide gel electrophoresis ; Matrix assisted laser desorption ionization - mass spectrometry ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Protein extract from yeast cells growing exponentially in saline medium was separated by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE), with the separation in the first dimension on a wide range immobilized pH (3-10) gradient. From one preparative 2-D gel a number of previously identified proteins were used as test material for our initial matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS) efforts on large scale rapid protein spot identification. Sample preparation via in-gel trypsin digestion was slightly modified to be compatible to MS analysis, and via this modified procedure MS generated peptide mass profiles could, in most cases with good precision, identify the protein in question. Preferential ionization was tested on a yeast aldehyde dehydrogenase (ALD7), and it was shown that the ionization of some peptides was clearly suppressed by the presence of others. Roughly 50% of the observed peptide masses was found by the search routines in the database, and the mass measurement accuracy of the peptides was within 0.5 Da. Silver-stained gels could be used with good results for the generation of peptides to be analyzed by MALDI-MS. For one of the 2-D resolved proteins, glycerol 3-phosphatase (GPP1), the post-source decay (PSD) spectrum proved crucial in identification.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180316
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