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The term matrix-assisted laser desorption ionization (MALDI) was coined in 1985 by Franz Hillenkamp, Michael Karas and their colleagues. [3] These researchers found that the amino acid alanine could be ionized more easily if it was mixed with the amino acid tryptophan and irradiated with a pulsed 266 nm laser.
Utility for proteomics designed to support the preprocessing and analysis of MALDI-TOF mass spectrometry data that loads data from mzML, mzXML and CSV files. It allows users to apply baseline correction, normalization, smoothing, peak detection and peak matching.
It is a variation of matrix-assisted laser desorption/ionization (MALDI). [ 1 ] [ 2 ] In MALDI, the sample is mixed with a matrix material and applied to a metal plate before irradiation by a laser, [ 3 ] whereas in SELDI, proteins of interest in a sample become bound to a surface before MS analysis.
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The surface-enhanced laser desorption/ionization (SELDI) variant is similar to MALDI, but uses a biochemical affinity target. [18] [19] The technique known as surface-enhanced neat desorption (SEND) [18] is a related variant of MALDI with the matrix is covalently linked to the target surface. The SELDI technology was commercialized by Ciphergen ...
MALDI mass spectrometry imaging (MALDI-MSI) is the use of matrix-assisted laser desorption ionization as a mass spectrometry imaging [2] technique in which the sample, often a thin tissue section, is moved in two dimensions while the mass spectrum is recorded. [3]
More than 50 years ago, MSI was introduced using secondary ion mass spectrometry (SIMS) to study semiconductor surfaces by Castaing and Slodzian. [5] However, it was the pioneering work of Richard Caprioli and colleagues in the late 1990s, demonstrating how matrix-assisted laser desorption/ionization (MALDI) could be applied to visualize large biomolecules (as proteins and lipids) in cells and ...
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