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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.
Easotope software archives, organizes, and analyzes mass spectrometer data. It is currently oriented toward clumped CO 2 analysis but is also useful for bulk CO 2 work and expandable to other isotopic systems. El-MAVEN Open-source Desktop software by Elucidata processes labeled LC-MS, GC-MS and LC-MS/MS data in open-formats (mzXML, mzML, CDF).
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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]
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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.
A typical workflow of a peptide mass fingerprinting experiment. Peptide mass fingerprinting (PMF), also known as protein fingerprinting, is an analytical technique for protein identification in which the unknown protein of interest is first cleaved into smaller peptides, whose absolute masses can be accurately measured with a mass spectrometer such as MALDI-TOF or ESI-TOF. [1]