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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Microcolumn Separations 1 (1989), S. 223-229 
    ISSN: 1040-7685
    Keywords: CZE-MS ; electrospray ionization ; peptides ; proteins ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Capillary zone electrophoresis (CZE) coupled with an on-line mass spectrometric (MS) detection system by an atmospheric pressure electrospray ionization (ESI) interface has been used successfully for Separations of peptide and protein mixtures. For CZE-MS, ESI produces multiply charged molecular ions and thus allows mas spectrometers with a limited mass-to-charge range to analyze proteins having molecular weights greater than 100,000. Various pH buffer systems have been investigated, including buffer systems in which pH 〉 pI (isoelectric point of analytes) and pH « pI are designed to reduce protein adsorption onto silica capillary surfaces and thus improve separation efficiencies. More than 125,000 theoretical plates have been obtained from a CZE-MS separation of less than 1 pmol per component of leucine enkephalin and horse heart myoglobin. CZE-MS of other large peptides and proteins are demonstrated.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Microcolumn Separations 5 (1993), S. 57-62 
    ISSN: 1040-7685
    Keywords: capillary electrophoresis ; electrospray ionization ; mass spectrometry ; reduced field strength ; peptides ; proteins ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A combined capillary electrophoresis/mass spectrometry (CE/MS) method is described that provides an increase in the efficiency of analysis by decreasing the analyte elution rate into an electrospray ionization (ESI) interface. The method is readily implemented by instituting a step change in the CE electric field strength for desired periods of time during a separation. As a result, the m/z range or the number of times an m/z range can be scanned while a solute elutes is increased by a factor proportional to the decrease in CE electric field strength. In addition, the method is shown not to cause any significant loss in separation quality as demonstrated for mixtures of proteins and peptides, while providing an effective gain in sensitivity. This allows an enhancement in the quality of mass spectra recorded while scanning wide m/z ranges. Mass spectra for a set of standard proteins were obtained for injections of 60 femtomole/protein, while analysis of an albumin tryptic digest was obtained for injections corresponding to 40 femtomoles of protein.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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