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  • Articles: DFG German National Licenses  (4)
  • 1995-1999  (4)
  • 1
    Electronic Resource
    Electronic Resource
    Matrix Dependence of Metastable Fragmentation of Glycoproteins in MALDI TOF Mass Spectrometry (1995)
    s.l. : American Chemical Society
    Analytical chemistry 67 (1995), S. 675-679 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac00099a029
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    High-Sensitivity Peptide Mapping by Micro-LC with On-Line Membrane Blotting and Subsequent Detection by Scanning-IR-MALDI Mass Spectrometry (1997)
    Springer
    The protein journal 16 (1997), S. 349-362 
    Details
    ISSN: 1573-4943
    Keywords: Scanning-IR-MALDI-MS ; sequencing ; ESI-MS ; peptide mapping ; micro-LC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A novel approach to the on-line mass determination of peptides from digested proteins by scanning infrared matrix-assisted laser desorption/ionization (scanning-IR-MALDI) is described. The peptides were continuously collected directly onto a PVDF (polyvinylidene fluoride) strip during a HPLC run. Individual peptides were detected by lining up the PVDF strip with the UV trace from the HPLC run, using visible dye markers as reference points. The local resolution of the peptides on the PVDF membrane is preserved during matrix incubation for MALDI-MS as shown by comparing the UV chromatogram and the total ion current (TIC) from an on-line coupled electrospray ionization (ESI) mass spectrometer with the scanning-IR-MALDI data from the corresponding areas on the PVDF strip. The intensities of the mass profiles obtained by scanning-IR-MALDI reflect the amount of peptides present on the PVDF strip. The higher sensitivity of IR-MALDI-MS yielded mass information not detectable by ESI-MS. After the scanning-IR-MALDI experiment, the same membrane strip can be used directly for automated Edman degradation. Comparable initial and repetitive yields were obtained for blotted peptides with and without matrix incubation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026324419398
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) of membrane proteins and non-covalent complexes (1995)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 30 (1995), S. 1462-1468 
    Details
    ISSN: 1076-5174
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Matrix-assisted laser desorption/ionization (MALDI) mass spectra and methods to improve their quality are reported for three hydrophobic, membrane-bound proteins: porin from Escherichia coli, bacteriorhodopsin from Halobacterium salinarium and cholesterolesterase from Pseudomonas fluorescens. Several commonly used UV and IR matrices have been tested. In addition, the susceptibility of MALDI mass spectrometry to various neutral and ionic detergents, known usually to degrade the quality of MALDI mass spectra, has been tested systematically. For porin, consisting of three identical non-covalently bound subunits, a new sample preparation is reported, resulting in the desorption of the intact quaternary protein structure. This leads to a better understanding of the way a given analyte is embedded into the host matrix crystals.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jms.1190301012
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Ultraviolet matrix assisted laser desorption ionization-mass spectrometry of electroblotted proteins (1996)
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 954-961 
    Details
    ISSN: 0173-0835
    Keywords: Mass determination ; Matrix-assisted laser desorption ionization-mass spectrometry ; Electroblotting ; Protein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Direct mass spectrometric analysis of proteins electroblotted onto polyvinylidene fluoride membranes after sodium dodecyl sulfate-polyacrylamide gel electrophoresis is demonstrated by matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS) with a linear time-of-flight instrument, equipped with a nitrogen laser (337 nm). The blotted proteins were desorbed directly from the blotting membrane after incubation with sinapinic acid as matrix. Different commercially available membranes resulted in high quality protein signals for hydrophobic membranes exhibiting high specific surface areas (Immobilon PSQ or Trans-Blot) or for charged membranes (Immobilon CD). Systematic investigations with standard proteins were performed to compare standard preparation procedures for ultraviolet (UV) MALDI-MS on stainless steel sample stages and preparation of proteins immobilized onto membranes either by direct application from protein solutions (spotting) or by electrotransfer from gels (electroblotting). Aspects such as mass resolution, reproducibility from shot to shot and spot to spot, mass accuracy, and preservation of protein localization are addressed in this paper.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150170518
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    Paper (German National Licenses)
    Fulltext
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