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And matrix-assisted laser desorption ionization

Anke, G. H., Thomas, M., Frank, G., Reiner, S., Helge, B., Markus, K., and Monika, K. (2008). Challenging the problem of clostridial identification with matrix-assisted laser desorption and ionization-time-of-fight mass spectrometry (MALDl-TOF MS). Anaerobe 14, 242-249. [Pg.123]

Proteins and other large biomolecules can be analyzed using MALDI (matrix-assisted laser desorption and ionization) with TOF... [Pg.780]

In 1988-1989, two processes were discovered that allowed the transfer of large molecules into the gas phase matrix-assisted laser desorption and ionization (MALDI) and electrospray ionization (Karas and Hillenkamp, 1988 Fenn et al., 1989). [Pg.2]

Schiller, J. Suss, R. Amhold, J. Fuchs, B. Lessig, J. Muller, M. Petkovic, M. Spalteholz, H. Zschomig, O. Arnold, K. Matrix-assisted laser desorption and ionization time-of-flight (MALDI-TOF) mass spectrometry in lipid and phospholipid research. Prog. Lipid Res. 2004, 43, 449-488. [Pg.60]

Figure 6 The SELDI technology. This type of proteomic analytical tool is a class of mass spectroscopy instrument that is useful in high-throughput proteomic fingerprinting of serum. Using a robotic sample dispenser, 1 p,L of serum is applied to the surface of a protein-binding chip. A subset of the proteins in the sample binds to the surface of the chip. The bound proteins are treated with a matrix-assisted laser desorption and ionization matrix and are washed and dried. The chip, which contains multiple patient samples, is inserted into a vacuum chamber where it is irradiated with a laser. The laser desorbs the adherent proteins and causes them to be launched as ions. The TOF of the ion before detection by an electrode is a measure of the mass-to-charge (m/z) value of the ion. The ion spectra can be analyzed by computer-assisted tools that classify a subset of the spectra by characteristic patterns of relative intensity (adapted from www.evmsdoctors.com). Figure 6 The SELDI technology. This type of proteomic analytical tool is a class of mass spectroscopy instrument that is useful in high-throughput proteomic fingerprinting of serum. Using a robotic sample dispenser, 1 p,L of serum is applied to the surface of a protein-binding chip. A subset of the proteins in the sample binds to the surface of the chip. The bound proteins are treated with a matrix-assisted laser desorption and ionization matrix and are washed and dried. The chip, which contains multiple patient samples, is inserted into a vacuum chamber where it is irradiated with a laser. The laser desorbs the adherent proteins and causes them to be launched as ions. The TOF of the ion before detection by an electrode is a measure of the mass-to-charge (m/z) value of the ion. The ion spectra can be analyzed by computer-assisted tools that classify a subset of the spectra by characteristic patterns of relative intensity (adapted from www.evmsdoctors.com).
Matrix assisted laser desorption and ionization (MALDI) technique has developed in 1987.269 270 Since then, it has proven to be one of the most successful ionization methods for the mass spectrometric investigation of large molecules, increasing the... [Pg.168]

It is even possible to kick out , like soccer balls, the neutral giant molybdenum oxide spheres, for example the Mo72Fe3o ones, into the gas phase using all matrix-assisted laser desorption and ionization (MALDI) methods. It is important that the clusters range from dimers to pentamers (see Figure 14.13) [17]. [Pg.463]

MALDI-TOF — Matrix-Assisted Laser Desorption and Ionization Time-of-FIight... [Pg.873]

Matrix-assisted laser desorption and ionization mass spectrometry was developed at the end of the 80s of the last century independent by Japanese and German scientists and is nowadays primarily used in protein and peptide research, but also for the analysis of carbohydrates and DNA. A detailed survey of the different applications of MALDI-TOF MS is provided in the excellent... [Pg.543]

Benard, S., Arnhold, J., Lehnert, M., Schiller, J. and Arnold, K., Experiments towards quantification of saturated and polyunsaturated diacylglycerols by matrix-assisted laser desorption and ionization time-of-flight mass spectrometry (MALDI-TOE MS), Chem Phys Lipids, 100 (1999) 115-125. [Pg.561]

Figure 9.2 The basic components of a mass spectrometer. All mass spectrometers consist of an ion source linked to a mass analyser then to a detector. The important ion sources and mass analysers for biological mass spectrometry are listed. There are many other potential ion sources and mass analysers used generally in mass spectrometry, but only the indicated are of use in the analysis of biological macromolecules and amphiphilic lipids, and also in proteomics FAB fast atom bombardment MALDI matrix-assisted laser desorption and ionization ESI electrospray ionization ToF time of flight FTICR fourier transform ion cyclotron resonance MS/MS tandem mass spectrometry. Figure 9.2 The basic components of a mass spectrometer. All mass spectrometers consist of an ion source linked to a mass analyser then to a detector. The important ion sources and mass analysers for biological mass spectrometry are listed. There are many other potential ion sources and mass analysers used generally in mass spectrometry, but only the indicated are of use in the analysis of biological macromolecules and amphiphilic lipids, and also in proteomics FAB fast atom bombardment MALDI matrix-assisted laser desorption and ionization ESI electrospray ionization ToF time of flight FTICR fourier transform ion cyclotron resonance MS/MS tandem mass spectrometry.
MALDI (matrix assisted laser desorption and ionization) combined with size-exclusion chromatography is increasingly being used to study the microstructure of polymers [542-544], MALDI allows the desorption and ionization of macromolecules with molecular mass up to hundreds of kilodaltons with little or no fragmentation. The MALDI mass spectra provides structural information for identification of the polymer repeat units or copolymer sequence, end group mass and mechanism of polymerization for polymers with a narrow polydispersity (< 1.25). For samples of high polydispersity MALDI fails to provide reliable information. The separation of polydisperse samples by size-exclusion chromatography provides fractions suitable for characterization by MALDI. MALDI can also be used for mass calibration of size-exclusion columns. [Pg.361]

Waters Corporation Synapt. The samples are solutions of biological material, and the ion sources are uniformly EIS, nanospray ionization, or matrix-assisted laser desorption and ionization as described in Chapters 4,9,15, and 18. Studies with the Synapt traveling wave instrument have revealed details of biomolecular ions in the gas phase that are not available by MS alone or by other methods. The full meaning of such studies and relevance for in vivo biomolecular activity is currently under discussion and debate " nonetheless, IM-MS for explorations of biomolecules certainly has affected the visibility of mobility as a measurement method and the level of technology that has been advanced through pharmaceutical and medical concerns. [Pg.13]

MALDI-TOF MS matrix-assisted laser desorption and ionization time of flight mass spectroscopy. ... [Pg.587]

Cramer, R., Hillenkamp, H., and Haglund, R. F. Jr., Infrared Matrix-Assisted Laser Desorption and Ionization by Using a Tunable Mid-Infrared Free-Electron Laser, /. Am. Soc. Mass Spectrom., 7, 1187, 1996. [Pg.511]

Mass spectrometry currently has assumed a central role in protein sequencing. This development has been possible with the introduction of two highly sensitive ionization techniques electrospray ionization (ESI) and matrix-assisted laser desorption and ionization (MALDI) and the advent of improved instrumentation capable of high-mass and high-sensitivity detection. Currently, biopolymers with a molecular mass over 100,000 Da are analyzed routinely. In the past, fast atom bombardment (FAB) [6,7] and Cf plasma desorption (PD) ionization [8] also played a limited role in protein sequencing. Mass spectrometry now has assumed... [Pg.293]

Matrix-assisted laser desorption and ionization process with mass spectrometric detection, which has been applied, for instance, for the identification of proteins and biological macromolecules. [Pg.2455]

MALDl Matrix-assisted laser desorption and ionization MS Mass spectromehy... [Pg.305]

Structural characterizations of macrocycUc aromatic sulfide oUgomers were studied jointly at Guangzhou Institute of Chemistry and McGUl University Department of Chemistry. The studies used matrix-assisted laser desorption and ionization time of flight mass spectroscopy (MALD ITF-MS), which the researchers said was a powerful tool to analyze the macrocyclics [13]. [Pg.15]

Fuchs, B. 2012. Analysis of phospholipids and glycoUpids by thin layer chromatography-matrix assisted laser desorption and ionization mass spectrometry, J. Chromatogr. A, 1259 62-73. [Pg.14]


See other pages where And matrix-assisted laser desorption ionization is mentioned: [Pg.26]    [Pg.168]    [Pg.341]    [Pg.514]    [Pg.444]    [Pg.168]    [Pg.105]    [Pg.284]    [Pg.341]    [Pg.110]    [Pg.541]    [Pg.106]    [Pg.532]    [Pg.424]    [Pg.517]   


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Assisted Laser Desorption

Desorption and

Desorption ionization

Laser assisted

Laser desorption

Laser ionization

Laser ionizing

Lasers and

Matrix assisted

Matrix assisted desorption+ionization

Matrix assisted laser desorption and ionization MALDI)

Matrix assisted laser ionization

Matrix ionization

Matrix-assisted laser

Matrix-assisted laser desorption ionization

Matrix-assisted laser desorption/ionization and electrospray

Matrix-assisted laser-desorption

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