Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Separation and analysis of the glycoform populations of ribonuclease B using capillary electrophoresis (1992)
    Springer
    Glycoconjugate journal 9 (1992), S. 86-91 
    Details
    ISSN: 1573-4986
    Keywords: Capillary electrophoresis ; glycoforms ; oligomannose ; ribonuclease B
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The development of methods to separate, analyse and monitor changes in glycoform populations is essential if a more detailed understanding of the structure, function and processing of glycoproteins is to emerge. In this study, intact ribonuclease B was resolved by borate capillary electrophoresis into five populations according to the particular oligomnnose structure associated with each glycoform. The relative proportions of these populations are correlated with the percentages obtained indirectly by analysis of the hydrazine released oligosaccharides using Bio-Gel P-4 gel filtration, matrix assisted laser desorption mass spectrometry and high performance anion exchange chromatography. Alterations in the composition of the glycoform populations during digestion of ribonuclease B withA. saitoi α(1–2)mannosidase were monitored by capillary electrophoresis (CE). Digestion of the free oligosaccharides under the same conditions, monitored by anion exchange chromatography, revealed a difference in rate, allowing some insight into the role of the protein during oligosaccharide processing. In conjunction with other methods, this novel application of CE may prove a useful addition to the techniques available for the study of glycoform populations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731704
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Characterisation of tissue-specific oligosaccharides from rat brain and kidney membrane preparations enriched in Na+,K+-ATPase (1999)
    Springer
    Glycoconjugate journal 16 (1999), S. 437-456 
    Details
    ISSN: 1573-4986
    Keywords: glycosylation ; Na+,K+-ATPase ; oligomannose ; polylactosamine ; tissue-specific ; 2-AB, 2-aminobenzamide ; AMOG, adhesion molecule on glia ; ATP, adenosine triphosphate ; BSA, bovine serum albumin ; CAM, calcium/calmodulin-dependent protein kinase ; CNS, central nervous system ; DSA, Datura stramonium agglutinin (lactosamine and sialic acid recognition) ; EDTA, ethylenediaminetetra-acetic acid ; Gal, galactose ; Glc-NAc, N-acetyl-D-glucosamine ; GNA, Galanthus nivalis agglutinin (oligomannosidic recognition) ; GnT, N-acetylglucosaminyltransferase ; GU, glucose unit ; HPLC, high performance liquid chromatography ; MALDI, matrix-assisted laser desorption/ionisation ; (Man)5–9, oligomannose-type glycan series with 5–9 manose residues ; Man1, Manβ1-4GlcNAcβ1-4 GlcNAc ; Man3, trimannose-chitobiose core ; Man3F, trimannose-chitobiose core with fucose on reducing terminal GlcNAc ; MS, mass spectrometry ; NP normal phase ; PBS, phosphate buffered saline ; PNGase F, protein-N-glycosidase F ; PVDF, poly(vinylidene difluoride) ; SDS-PAGE, sodium dodecyl sulphate polyacrylamine gel electrophoresis ; TOF, time-of-flight ; Tris, 2-amino-2-hydroxymethylpropane-1,3 diol ; WAX, weak anion exchange
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The organ-specific nature of the glycosylation of Na+,K+-ATPase-enriched preparations from kidney and brain tissues has earlier been indicated by the use of lectin-staining techniques. Na+,K+-ATPase is ubiquitous and abundant, and subject to upregulation during cell-division and in certain pathological conditions. Lectins specific for the different carbohydrates displayed by the Na+,K+-ATPases may, therefore, be useful carriers/mediators in tissue-specific targeting. N-linked oligosaccharides purified from Na+,K+-ATPase-enriched preparations from rat brain and kidney were consequently characterised in detail in this study using weak anion exchange and normal phase HPLC (combined with serial glycosidase digestions) and matrix-assisted laser desorption/ionisation mass spectrometry. The oligomannose series of glycans were most abundant in the brain tissue preparation and this contrasted with the renal-associated oligosaccharides that were dominated by families of tetra-antennary glycans (with/without a core fucose) with up to four lactosaminylglycan residues in either branched or linear formation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007078511110
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Structural determination of N-linked carbohydrates by matrix-assisted laser desorption/ionization-mass spectrometry following enzymatic release within sodium dodecyl sulphate-polyacrylamide electrophoresis gels: Application to species-specific glycosylation of α1-acid glycoprotein (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 1950-1959 
    Details
    ISSN: 0173-0835
    Keywords: Carbohydrates ; Matrix assisted laser desorption ; ionization-mass spectrometry ; Sodium dodecyl sulfate - polyacrylamide gel electrophoresis ; Peptide N-glycosidase P ; α1-Acid glycoprotein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: This paper describes a sensitive method for analysis of N-linked carbohydrates released enzymatically from within the gel following separation of glycoproteins (50-100 pmols) by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The separated bands containing the glycoproteins were cut from the gel, destained, reduced and alkylated. N-linked glycans were then released by in-gel incubation with peptide N-glycosidase-F (PNGase-F) and extracted with water and acetonitrile. Sialic acid-containing glycans were converted into methyl esters by reaction with methyl iodide, salts and reagents were removed by passage through a mixed-bed column of ion-exchange resins and the glycans were examined by matrix-assisted laser desorption/ionization (MALDI)-mass spectrometry. Structural determination of the released glycans was performed by exoglycosidase digestion. Following glycan release and extraction, the protein could be digested within the gel with trypsin, and the masses of the tryptic peptides could be compared with those generated from a sequence database for protein identification. The method is applied to the analysis of N-linked glycans from α1-acid glycoprotein from man, cow, sheep and dog. Major species-specific differences in glycosylation were found. Thus, although all four species used N-acetyl-neuraminic acid, only cow and sheep additionally used N-glycolyl-neuraminic acid. Biantennary glycans were the predominant carbohydrates in cow, sheep and dog but man produced more triantennary glycans and a substantial amount of tetraantennary sugars. Fucosylation was only found in glycans from man and cow and both cow and sheep glycans were found to have β1-3- and well as β1-4-linked galactose residues in the antennae.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191113
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...