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  • 1
    Electronic Resource
    Electronic Resource
    Threshold conditions of plasma ignition in laser ionization mass spectrometry of solids (1989)
    s.l. : American Chemical Society
    Analytical chemistry 61 (1989), S. 1029-1035 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac00184a007
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Accurate Mass Measurements Using MALDI-TOF with Delayed Extraction (1997)
    Springer
    The protein journal 16 (1997), S. 363-369 
    Details
    ISSN: 1573-4943
    Keywords: Accurate mass ; MALDI-TOF ; delayed extraction ; mass spectrometry ; peptide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry is now an essential tool in biopolymer analysis. Sensitivity and mass range are unsurpassed, but mass measurement accuracy and resolution have been limited. With delayed extraction and a reflecting analyzer, mass measurements using MALDI-TOF can be made with an accuracy of a few parts per million (ppm). It is possible to distinguish Lys from Gln in peptides, and to determine the elemental composition of smaller molecules (mass 100–500). In database searching strategies, a smaller mass window, resulting from an increase in mass accuracy, greatly decreases the number of possible candidates. Mass measurement accuracy with errors less than 5 ppm is demonstrated on a mixture of 12 peptides ranging in mass from ca. 900 to 3700 Da. Mass measurements on 13 peaks in an unseparated tryptic digest of myoglobin gave results with an overall average error less than 3.5 ppm, with a maximum error of 7 ppm.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026376403468
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  • 3
    Electronic Resource
    Electronic Resource
    Generation of large radical ions from oligometallocenes by matrix-assisted laser desorption ionization (1993)
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 7 (1993), S. 343-351 
    Details
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: Non-polar polymers containing ferrocene, ferrocenylnaphthalene, and ruthenocenylnaphthalene groups in their repeating units were studied by matrix-assisted laser desorption ionization (MALDI) time-of-flight mass spectrometry. Sample preparation for these polymers utilized tetrahydrofuran as solvent and several new matrices such as dithranol, 9-nitroanthracene, and quinizarin (all of these are anthracene derivatives). By comparing the mass spectra of oligometallocenes recorded with different matrices at different wavelengths (337 nm and 2.94 μm) and laser desorption ionization mass spectra recorded without matrix, it could be verified that the major analyte-related peaks in the MALDI mass spectra corresponded to the radical molecular ions. Radical ions have not been seen in the MALDI mass spectra of biopolymers such as proteins, peptides, and carbohydrates. Radical formation was demonstrated for samples in the mass range (1 kDa-13 kDa). Even in the presence of potential cationization sites such as methyl ester groups in the repeating units of some polyferrocene samples, MALDI mass spectra were dominated by radical ions of the analyte. Two possible mechanisms for radical formation in MALDI are discussed. Comparison of results with different matrices suggested that the distribution of masses observed in the mass spectra and characterized by the polydispersity index was independent of the matrix, but significant differences (5%) in the average molecular weights of the mass distributions were found.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/rcm.1290070508
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  • 4
    Electronic Resource
    Electronic Resource
    Sensitivity and mass accuracy for proteins analyzed directly from polyacrylamide gels: Implications for proteome mapping (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 382-390 
    Details
    ISSN: 0173-0835
    Keywords: Polyacrylamide gel ; Matrix-assisted laser desorption ; ionization ; Membranes ; Mass spectrometry ; Blotting ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Matrix-assisted laser desorption ionization (MALDI) mass spectra have been obtained directly from thin-layer isoelectric focusing (IEF) gels with as little as 700 femtomoles of α- and β-chain bovine hemoglobin and bovine carbonic anhydrase, and 2 picomoles of bovine trypsinogen, soybean trypsin inhibitor, and bovine serum albumin all loaded onto a single lane. By soaking the gel in a matrix solution, matrix was deposited over the entire gel surface, allowing MALDI scanning down complete lanes of the one-dimensional gel. As long as matrix crystals were deposited finely on the surface of the gel, time-lag focusing techniques were capable of ameliorating some of the mass accuracy limitations inherent in desorbing from uneven insulator surfaces with external calibration. Eleven measurements on the 5 kDa α-subunit proteins of lentil lectin measured over the course of 1 h and referenced to a single calibration yielded a standard deviation of 0.025%. Colloidal gold staining was found to be compatible with desorption directly from IEF and sodium dodecyl sulfate (SDS)-polyacrylamide gels. This direct approach simplifies the interface between gel electrophoresis and mass spectrometry dramatically, making the process more amenable to automation.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180312
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