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Laser Desorption Mass Spectrometry: History
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Contributor: Helena Kang

Laser desorption mass spectrometry uses a pulsed laser to release material from a condensed-phase sample and generate gas-phase ions for mass analysis. In direct laser desorption, the analyte or substrate absorbs the pulse; in matrix-assisted laser desorption/ionization (MALDI), an excess of a light-absorbing matrix co-crystallized with the analyte mediates energy deposition and ion formation [1]. Short irradiation produces a desorption plume containing neutrals, clusters, and ions, and subsequent proton-transfer, cationization, or deprotonation processes determine the detected species. The source is commonly coupled to a time-of-flight analyzer because pulsed ion production provides a natural start time, but the analyzer is not part of the defining ionization principle [2]. The method differs from electrospray, which forms ions from charged droplets, and from secondary-ion mass spectrometry, which uses a primary ion beam. Its essential features are pulsed photon irradiation, a localized condensed sample, desorption with ion formation, extraction of the plume ions, and mass-to-charge measurement.

  • laser desorption
  • MALDI
  • pulsed laser
  • desorption ionization

Mass Spectrometry Techniques and Applications • Spectroscopy • Chemistry • Physical Sciences

References

  1. Michael. Karas; Franz. Hillenkamp; Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal. Chem. 1988, 60, 2299-2301, 10.1021/ac00171a028.
  2. Andrej Shevchenko; Matthias Wilm; Ole Vorm; Matthias Mann; Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels. Anal. Chem. 1996, 68, 850-858, 10.1021/ac950914h.
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