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  • Biochemistry and Biotechnology  (3)
  • Wiley-Blackwell  (3)
  • Kiel: Kiel Institute of World Economics (IfW)
  • Frontiers Media
  • ZBW - Deutsche Zentralbibliothek für Wirtschaftswissenschaften, Leibniz-Informationszentrum Wirtschaft Kiel, Hamburg
  • Wiley
Collection
Keywords
Publisher
  • Wiley-Blackwell  (3)
  • Kiel: Kiel Institute of World Economics (IfW)
  • Frontiers Media
  • ZBW - Deutsche Zentralbibliothek für Wirtschaftswissenschaften, Leibniz-Informationszentrum Wirtschaft Kiel, Hamburg
  • Wiley
Years
  • 1
    Electronic Resource
    Electronic Resource
    Sample matrix effects on glycopeptide stability by high performance capillary electrophoresis (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 751-756 
    Details
    ISSN: 0173-0835
    Keywords: Glycopeptides ; Matrix ; Stability ; Capillary electrophoresis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: High performance capillary electrophoresis (CE) of glycoprotein digests frequently reveals extensive microheterogeneity associated with specific protein glycosylation sites. The choice of the sample matrix can influence the electrophoretic migration time, peak shape and resolution, as well as the physical stability of the product glycopeptides. Acetic acid is a frequently employed sample matrix for both capillary electrophoresis and electrospray ionization-mass spectrometry (ESI-MS). Acetic acid appears to enhance the spontaneous hydrolysis of sialic acids from the nonreducing termini of glycopeptides in a time- and concentration-dependent manner, even at 5°C, as evidenced by changes in the electrophoretic mobility and ESI-MS spectra of the resulting glycopeptides. The observed parallel electrophoretic mobility changes for specific glycoforms are consistent with the induction of peptide structure with time. Asialoglycopeptide mobilities were stable in acetic acid. Electrophoretic mobilities can be stabilized with propionic acid sample matrix with no apparent structural changes observed by ESI-MS within 31 h. Migration time reproducibility was in the range of 0.1% relative standard deviation (N = 7) with excellent peak shapes and enhanced glycopeptide resolution.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180515
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  • 2
    Electronic Resource
    Electronic Resource
    Peptide capillary zone electrophoresis mass spectrometry of recombinant human erythropoietin: An evaluation of the analytical method (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 2654-2664 
    Details
    ISSN: 0173-0835
    Keywords: Glycoprotein ; Glycopeptide ; Peptide ; Capillary electrophoresis ; Mass spectrometry ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: An evaluation of capillary zone electrophoresis-mass spectrometry (CZE-MS) as an analytical methodology for the separation and characterization of complex glycopeptides and nonglycopeptide structures has been performed. The evaluation employed endoproteinase V8 digested recombinant human erythropoietin (rHuEPO) that was further fractionated by reverse phase chromatography. The peptides were subjected to sequence analysis and evaluated by capillary electrophoresis, with or without mass detection, for peptide purity. The peptide mass determined from the sequence was then compared to the mass obtained from CZE-MS. Glycosylation sites and carbohydrate branch patterns were easily determined, site specific microheterogeneity (either O-acetylation of N-acetylneur-aminic acids or lactosamine extensions of the carbohydrate chain length) was assessed directly, glycosylation site occupancy was evaluated qualitatively, and nonglycopeptides were resolved and analyzed on-line with ease. Incomplete peptide digestion products were detected and identified by CZE-MS. Protein sequence coverage by CZE-MS was 98.2 percent complete from a single map. Offline evaluation of peptide purity by CZE greatly aided the interpretation of multiple sequence analysis and, in validating that, the CZE-MS was detecting all peptides present. All off-line CZE and on-line CZE-MS experiments employed a capillary that was dynamically coated with Polybrene in the presence of polyethylene glycol; separations were conducted in 0.67 M formic acid.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191515
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  • 3
    Electronic Resource
    Electronic Resource
    Use of a Hepta-tyr glycopeptide antibiotic as chiral selector in capillary electrophoresis (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 1742-1751 
    Details
    ISSN: 0173-0835
    Keywords: Antibiotics ; Chiral separations ; Enantiomers ; Drugs ; Herbicides ; Capillary electrophoresis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A new glycopeptide antibiotic, MDL 63,246 (Hepta-tyr), of the teicoplanin family, has been evaluated in capillary electrophoresis for the resolution of chiral compounds of pharmaceutical and environmental interest. Electrophoretic separations were carried out in a polyacrylamide-coated capillary using the partial filling-counter current mode with aqueous-organic buffers in the pH range 4-6. Experimental parameters affecting resolution, such as antibiotic concentration, buffer pH, organic modifier type and capillary temperature, were studied. The Hepta-tyr antibiotic exhibited a high enantiorecognition capability towards the studied compounds at very low concentrations (1-2 mg/mL). The optimum experimental conditions were achieved by using a buffer at pH 5 containing acetonitrile at 25°C.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191036
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