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Alan G Marshall - One of the best experts on this subject based on the ideXlab platform.

  • structural characterization of phospholipids by matrix assisted Laser desorption ionization fourier transform ion cyclotron resonance mass spectrometry
    Analytical Chemistry, 1995
    Co-Authors: Jarrod A Marto, Forest M White, Staci Seldomridge, Alan G Marshall
    Abstract:

    Matrix-Assisted Laser desorption/ionization (MALDI) Fourier transform ion cyclotron resonance mass spectrometry provides for structural analysis of the principal biological phospholipids : glycerophosphatidylcholine, -ethanolamine, -serine, and -inositol. Both positive and negative molecular or quasimolecular ions are generated in high abundance. Isolated molecular ions may be collisionally activated in the source side of a dual trap mass analyzer, yielding fragments serving to identify the polar head group (positive ion mode) and fatty acid side chains (negative ion mode). Azimuthal quadrupolar excitation following collisionally activated dissociation refocuses product ions close to the solenoid axis ; subsequent transfer of product ions to the analyzer ion trap allows for high-resolution mass analysis. Cyro-cooling of the sample probe with liquid nitrogen greatly reduces matrix adduction encountered in the negative ion mode.

J F Muller - One of the best experts on this subject based on the ideXlab platform.

  • evaluation of combined matrix assisted Laser desorption ionization time of flight and matrix assisted Laser desorption ionization fourier transform ion cyclotron resonance mass spectrometry experiments for peptide mass fingerprinting analysis
    Rapid Communications in Mass Spectrometry, 2011
    Co-Authors: David Da Silva, Thierry Wasselin, Vincent Carre, Patrick Chaimbault, Lina Bezdetnaya, Benoit Maunit, J F Muller
    Abstract:

    Peptide Mass Fingerprinting (PMF) is still of significant interest in proteomics because it allows a large number of complex samples to be rapidly screened and characterized. The main part of post-translational modifications is generally preserved. In some specific cases, PMF suffers from ambiguous or unsuccessful identification. In order to improve its reliability, a combined approach using Matrix-Assisted Laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) and Matrix-Assisted Laser desorption/ionization Fourier transform ion cyclotron resonance mass spectrometry (MALDI-FTICRMS) was evaluated. The study was carried out on bovine serum albumin (BSA) digest. The influence of several important parameters (the matrix, the sample preparation method, the amount of the analyte) on the MOWSE score and the protein sequence coverage were evaluated to allow the identification of specific effects. A careful investigation of the sequence coverage obtained by each kind of experiment ensured the detection of specific peptides for each experimental condition. Results highlighted that DHB-FTICRMS and DHB- or CHCA-TOFMS are the most suited combinations of experimental conditions to achieve PMF analysis. The association (convolution) of the data obtained by each of these techniques ensured a significant increase in the MOWSE score and the protein sequence coverage. Copyright © 2011 John Wiley & Sons, Ltd.

Jarrod A Marto - One of the best experts on this subject based on the ideXlab platform.

  • structural characterization of phospholipids by matrix assisted Laser desorption ionization fourier transform ion cyclotron resonance mass spectrometry
    Analytical Chemistry, 1995
    Co-Authors: Jarrod A Marto, Forest M White, Staci Seldomridge, Alan G Marshall
    Abstract:

    Matrix-Assisted Laser desorption/ionization (MALDI) Fourier transform ion cyclotron resonance mass spectrometry provides for structural analysis of the principal biological phospholipids : glycerophosphatidylcholine, -ethanolamine, -serine, and -inositol. Both positive and negative molecular or quasimolecular ions are generated in high abundance. Isolated molecular ions may be collisionally activated in the source side of a dual trap mass analyzer, yielding fragments serving to identify the polar head group (positive ion mode) and fatty acid side chains (negative ion mode). Azimuthal quadrupolar excitation following collisionally activated dissociation refocuses product ions close to the solenoid axis ; subsequent transfer of product ions to the analyzer ion trap allows for high-resolution mass analysis. Cyro-cooling of the sample probe with liquid nitrogen greatly reduces matrix adduction encountered in the negative ion mode.

Richard M. Caprioli - One of the best experts on this subject based on the ideXlab platform.

  • matrix assisted Laser desorption ionization imaging mass spectrometry in situ molecular mapping
    Biochemistry, 2013
    Co-Authors: Peggi M Angel, Richard M. Caprioli
    Abstract:

    Matrix-Assisted Laser desorption ionization imaging mass spectrometry (IMS) is a relatively new imaging modality that allows mapping of a wide range of biomolecules within a thin tissue section. The technology uses a Laser beam to directly desorb and ionize molecules from discrete locations on the tissue that are subsequently recorded in a mass spectrometer. IMS is distinguished by the ability to directly measure molecules in situ ranging from small metabolites to proteins, reporting hundreds to thousands of expression patterns from a single imaging experiment. This article reviews recent advances in IMS technology, applications, and experimental strategies that allow it to significantly aid in the discovery and understanding of molecular processes in biological and clinical samples.

  • direct tissue analysis using matrix assisted Laser desorption ionization mass spectrometry practical aspects of sample preparation
    Journal of Mass Spectrometry, 2003
    Co-Authors: Sarah A. Schwartz, Michelle L. Reyzer, Richard M. Caprioli
    Abstract:

    Practical guidelines for the preparation of tissue sections for direct analysis by Matrix-Assisted Laser desorption/ionization (MALDI) mass spectrometry are presented. Techniques for proper sample handling including tissue storage, sectioning and mounting are described. Emphasis is placed on optimizing matrix parameters such as the type of matrix molecule used, matrix concentration, and solvent composition. Several different techniques for matrix application are illustrated. Optimal instrument parameters and the necessity for advanced data analysis approaches with regards to direct tissue analysis are also discussed.

  • direct tissue analysis using matrix assisted Laser desorption ionization mass spectrometry practical aspects of sample preparation
    Journal of Mass Spectrometry, 2003
    Co-Authors: Sarah A. Schwartz, Michelle L. Reyzer, Richard M. Caprioli
    Abstract:

    Practical guidelines for the preparation of tissue sections for direct analysis by Matrix-Assisted Laser desorption/ionization (MALDI) mass spectrometry are presented. Techniques for proper sample handling including tissue storage, sectioning and mounting are described. Emphasis is placed on optimizing matrix parameters such as the type of matrix molecule used, matrix concentration, and solvent composition. Several different techniques for matrix application are illustrated. Optimal instrument parameters and the necessity for advanced data analysis approaches with regards to direct tissue analysis are also discussed. Copyright © 2003 John Wiley & Sons, Ltd.

Jennifer Dien Bard - One of the best experts on this subject based on the ideXlab platform.