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  • 1
    Electronic Resource
    Electronic Resource
    Performance of a fast atom bombardment source on a quadrupole mass spectrometer (1983)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 10 (1983), S. 94-97 
    Details
    ISSN: 0306-042X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A saddle field fast atom bombardment gun was installed on a quadrupole mass spectrometer and its performance evaluated. Only some minor modifications to a standard gas chromatography mass spectrometry system were required to accommodate this source. Using xenon as the bombarding atom, measurements were made with respect to sensitivity, background effects, sample type, calibration of the data system and other parameters pertinent to the operation of a fast atom bombardment source on a quadrupole system. The simplicity of operation and its unique ability to produce gaseous ionic species from highly polar molecules in solution make it an ideal complement to other mass spectrometric ionizing devices.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200100209
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Following enzyme catalysis in real-time inside a fast atom bombardment mass spectrometer (1983)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 10 (1983), S. 98-102 
    Details
    ISSN: 0306-042X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Experiments involving the monitoring of enzyme catalyzed reactions occurring within a fast atom bombardment mass spectrometer are reported. Data are presented using FAB mass spectrometry to monitor trypsin and dipeptidyl aminopeptidase I catalyzed hydrolysis of their respective assay substrates and for hydrolysis of the peptide (val4) angiotensin III by yeast carboxypeptidase Y. Enzyme catalysis was followed by measuring the decrease of abundance of the [M + H]+ ion of the substrate and the increase of that of the product from a mixture of enzyme and substrate in a glycerol/water matrix placed on the probe inside the mass spectrometer. In addition, results of preliminary experiments to determine the survival of live yeast cells on exposure to FAB mass spectrometry is also presented.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200100210
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Enzyme reaction rates determined by fast atom bombardment mass spectrometry (1984)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 11 (1984), S. 392-395 
    Details
    ISSN: 0306-042X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Fast atom bombardment (FAB) mass spectrometry has been used to measure the reaction rate of trypsin with the synthetic substrate p-toluenesulfonyl-L-arginine methyl ester (TAME). Rates were measured by FAB mass spectrometry both in real time by monitoring the reaction as it proceeded on the probe inside the mass spectrometer, and also by individual analysis of a series of aliquots removed with time from a batch reaction. The results were then compared to the rates measured using the usual spectrophotometric (UV) assay run with the same reaction mixture. The results showed that the initial rates of trypsin cleavage were the same for these three methods at approximately 0.15 μmol product produced min-1 μg-1 enzyme. After 5 min, the rates determined by FAB mass spectrometry using timed aliquots and the UV assay remained about the same, whereas the real-time measurement decreased substantially to approximately 0.002 μmol product min-1 μg-1 enzyme. The results are discussed with respect to the particular advantages and disadvantages of these methods for following enzyme reactions.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200110805
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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