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  • 1
    Electronic Resource
    Electronic Resource
    Characterization of glycosphingolipid mixtures with up to ten sugars by gas chromatography and gas chromatography-mass spectrometry as permethylated oligosaccharides and ceramides released by ceramide glycanase (1989)
    s.l. : American Chemical Society
    Biochemistry 28 (1989), S. 6672-6678 
    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/bi00442a021
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  • 2
    Electronic Resource
    Electronic Resource
    Determination of oligosaccharides in foods, diets, and intestinal contents by high-temperature gas chromatography and gas chromatography/mass spectrometry (1992)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 40 (1992), S. 2404-2412 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf00024a015
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular characterization of the large heavily glycosylated domain glycopeptide from the rat small intestinal Muc2 mucin (1996)
    Springer
    Glycoconjugate journal 13 (1996), S. 823-831 
    Details
    ISSN: 1573-4986
    Keywords: mucin ; rat small intestine ; sulfated oligosaccharides ; mmunolocalization ; goblet cell ; Muc2
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The largest high-glycosylated domain, glycopeptide A, of the ‘insoluble’ mucin complex of the rat small intestine has earlier been purified and characterized (Carlstedtet al., 1993,J Biol Chem 268: 18771–81). A rabbit antiserum raised against deglycosylated glycopeptide A was used to clone part of a mucin showing homology to the human MUC2 mucin (Hanssonet al., 1994,Biochem Biophys Res Commun 198: 181–90). This serum specifically stained goblet cells (paranuclear) in the mouse small intestine. The size of the coding sequence of glycopeptide A was estimated by using reversed transcriptase PCR of mRNA from an inbred rat strain (GOT-W) using primers in the unique central and C-terminal parts of the proposed rat Muc2 sequences. The PCR and Southern blot of the PCR products showed a fragment of about 5.5 kb corresponding to about 1700 amino acids when the known Cys-rich sequences used for the primers were subtracted. This is slightly larger than the size estimated earlier by biochemical studies. The mRNA encoding the rat Muc2 was slightly smaller than the mRNA encoding the human MUC2 in a colorectal cell line. Although the size of glycopeptide A estimated from biochemical results and by PCR is not identical, the results obtained here further support that the ‘insoluble’ mucin of the rat small intestine is encoded by the Muc2 gene. Most of the oligosaccharides in glycopeptide A were either neutral (40%) or sialylated (40%). The remaining ones were sulfated with the sulfate group attached to C-6 ofN-acetylglucosamine linked to C-6 of theN-acetylgalactosaminitol as revealed by tandem mass spectrometry of the perdeuteroacetylated oligosaccharides. Eighteen oligosaccharides were found of which fourteen were characterized and found to be mostly novel. Our findings thus expand the current knowledge of the core peptide of the rat intestinal goblet cell mucin and provide a relatively complete picture of the glycosylation of a defined mucin domain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00702346
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  • 4
    Electronic Resource
    Electronic Resource
    Different O-glycosylation of respiratory mucin glycopeptides from a patient with cystic fibrosis (1998)
    Springer
    Glycoconjugate journal 15 (1998), S. 823-833 
    Details
    ISSN: 1573-4986
    Keywords: mucin ; cystic fibrosis ; oligosaccharides ; MALDI ; GC-MS ; CF, cystic fibrosis ; GalNAcol, N-acetylgalactosaminitol ; Hex, hexose ; HexNAc, N-acetylhexosamine ; HexNAcol ; GC, gas chromatography ; MALDI, matrix-assisted laser ; FAB, fast atom bombardment ; MS, mass spectrometry ; CID,collision induced dissociation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The O-linked oligosaccharides from three fractions of highly glycosylated mucin glycopeptides obtained from sputum of a patient with cystic fibrosis were characterized and compared regarding size, composition, sequence and when possible linkage positions. Neutral and sialic acid-containing glycans were permethylated and analyzed by high-temperature GC-MS and MALDI-MS, showing more than 60 different oligosaccharides with a size of up to 15 monosaccharide units. Some of the observed oligosaccharides are novel for respiratory secretions, one being a trifucosylated heptasaccharide with the proposed structure: Fuc-Gal-4(Fuc-3)GlcNAc-(Fuc-)Gal-3GalNAcol. The glycosylation of two of the glycopeptide fractions was similar with regard to the neutral and sialylated oligosaccharides despite their different origins from the sol or gel phase. Analysis of the sulfated oligosaccharides by FAB-MS/MS indicated that the gel fraction contained C-6 linked sulfate groups while the two sol fractions also contained C-3 linked sulfate. The results suggest the presence of different glycosylated mucin domains, probably originating from different mucin glycoforms and/or apoproteins in the airway of cystic fibrosis patients.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006920219069
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  • 5
    Electronic Resource
    Electronic Resource
    Strategy for the investigation of O-linked oligosaccharides from mucins based on the separation into neutral, sialic acid- and sulfate-containing species (1995)
    Springer
    Glycoconjugate journal 12 (1995), S. 69-76 
    Details
    ISSN: 1573-4986
    Keywords: Gas chromatography-mass spectrometry ; oligosaccharide ; mucin ; high performance anion exchange chromatography ; sialic acid ; sulfate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A method for the separation of O-linked oligosaccharides into neutral, sialic acid-containing and sulfated species was applied to oligosaccharides released by alkaline borohydride from mucin glycopeptides from porcine small intestine. The released mixture of reduced oligosaccharides was applied to an anion exchange column, and the neutral oligosaccharides were collected as the unretarded fraction. A mixture of dimethyl sulfoxide and iodomethane was passed through the column to convert the sialic acid-containing oligosaccharides into methyl esters that were eluted and converted to methyl amides by methyl amine. Finally the sulfated oligosaccharide fraction was eluted with salt. The neutral and the derivatized sialic acid-containing oligosaccharides were analysed by gas chromatography-mass spectrometry after permethylation and the sulfated oligosaccharide fraction was analysed by high performance anion exchange chromatography.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731871
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  • 6
    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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