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  • Articles  (2)
  • Glycopeptides  (1)
  • Herbicides  (1)
  • 1995-1999  (2)
  • 1925-1929
  • 1
    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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  • 2
    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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