Mass spectrometry desorption ionization

Matrix-assisted Laser Desorption/ Ionization Mass Spectrometry... 

Fenn, J.B. et al.. Electrospray ion formation desorption versus desertion, m Biochemical and Biotechnological Applications of Electrospray Ionization Mass Spectrometry, ACS Symposium Series, Snyder, A.P. and Anaheim, C.A., Eds., Washington, D.C., 1995, chap. 3. 

Liquid chromatography/mass spectrometry Lower limit of detection Limit of detection Limit of quantitation Florseshoe crab hemocyanin Liquid scintillation counting Matrix-assisted laser desorption/ ionization mass spectrometry m -Maleimidobenzoy 1-A -Hydroxysuccinimide 1 -Cyclohexyl-3-(2-Morptiolino-ethyl)carbodiimide rnetlio-/ -Toluenesulfonate (same as CDI)... 

Hurst, G. Doktycz, M. Vass, A. Buchanan, M. Detection of bacterial DNA polymerase chain reaction products by matrix assisted laser desorption/ionization mass spectrometry. Rapid. Commun. Mass Spectrom. 1996,10,377-382. 

Hathout, Y. Demirev, P. A. Ho, Y.-P Bundy, J. L. Ryzhov, V. Sapp, L. Stutler, J. Jackman, J. Fenselau, C. Identification of Bacillus spores by matrix-assisted laser desorption ionization-mass spectrometry. Appl. Environm. Microbiol. 1999, 65, 4313-4319. 

Jarman, K. H. Cebula, S. T. Saenz, A. J. Peterson, C. E. Valentive, N. B. Kingsley, M. T. Wahl, K. L. An algorithm for automated bacterial identification using matrix-assisted laser desorption/ionization mass spectrometry. Anal. Chem. 2000, 72, 1217-1223. 

Nordhoff, E. Ingendoh, A. Cramer, R. Overberg, A. Stahl, B. Karas, M. Hillenkamp, F. Crain, P. F. Matrix-assisted laser desorption/ionization mass spectrometry of nucleic acids with wavelengths in the UV and IR. Rapid Comm. Mass Spectrom. 1992, 6,771-776. 

Liang, X. Zheng, K. Qian, M. G. Lubman, D. M. Determination of bacterial protein profiles by matrix-assisted laser desorption/ionization mass spectrometry with high-performance liquid chromatography. Rapid Comm. Mass Spectrom. 1996,10,1219-1226. 

Vaidyanathan, S. Winder, C. L. Wade, S. C. Kell, D. B. Goodacre, R. Sample preparation in matrix-assisted laser desorption/ionization mass spectrometry of whole bacterial cells and the detection of high mass (>20kDa) proteins. Rapid Comm. Mass Spectrom. 2002,16,1276-1286. 

Parker, C. E. Papac, D. L Tomer, K. B. Monitoring cleavage of fusion protein by matrix-assisted laser desorption ionization/mass spectrometry Recombinant HIV-1IIIB p26. Anal. Biochem. 1996, 239, 25-34. 

Arnold, R. J. Reilly, J. P. Observation of tetrahydrofolyl-poly-glutamic acid in bacteria cells by matrix assisted laser desorption/ionization mass spectrometry. Anal. Biochem. 2000,281,45-54. 

Pineda, F. J. Antoine, M. D. Demirev, P A. Feldman, A. B. Jackman, J. Longenecker, M. Lin, J. S. Microorganism identification by matrix-assisted laser/desorption ionization mass spectrometry and model-derived ribosomal protein biomarkers. Anal. Chem. 2003,75,3817-3822. 

Wingerath, T. et al. (1999). Analysis of cyclic and acyclic analogs of retinol, retinoic acid, and retinal by laser desorption ionization-, matrix-assisted laser desorption ionization-mass spectrometry, and UV/Vis. spectroscopy. Anal. Biochem. 272(2) 232-242. 

The most discriminating technique for proving the identity and purity of analyte peak of a chromatogram, especially for analyzing biological samples and natural products, is by using online LC-UV/MS or GC-MS/FTIR methods [15]. Alternatively, one could use a combination of TLC and MS, where direct determination on the TLC plates is made by matrix-assisted laser desorption ionization mass spectrometry (MALDI MS) [16]. 

Many diseases are characterized by the expression of specific proteins1 in some cases, malignant cells yield unique protein profiles when total cellular protein extracts are analyzed by proteomic methods such as two-dimensional gel electrophoresis or matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS).2 High-throughput proteomic studies may be useful to differentiate normal cells from cancer cells, to identify and define the use of biomarkers for specific cancers, and to characterize the clinical course of disease. Proteomics can also be used to isolate and characterize potential drug targets and to evaluate the efficacy of treatments. 

Schwartz S, Reyzer M, Caprioli R. Direct tissue analysis using matrix-assisted laser desorption/ionization mass spectrometry practical aspects of sample preparation. /. Mass. Spectrom. 2003 38 699-708. 

M. Schiirenberg, K. Dreisewerd, and F. Hillenkamp, Laser Desorption/Ionization Mass Spectrometry of Peptides and Proteins with Particle Suspension Matrices, Anal. Chem., 71, 221 229(1999). 

M.J. Dale, R. Knochenmuss, and R. Zenobi, Graphite/Liquid Mixed Matrices for Laser Desorption/Ionization Mass Spectrometry, Anal. Chem., 68, 3321 3329 (1996). 

Other MS based analytical approaches have occasionally been applied to ancient resin samples, in particular for paint varnishes. Such techniques include FABS (fast atom bombardment mass spectrometry) [35], MALDI (matrix assisted laser desorption-ionization mass spectrometry) and GALDI (graphite assisted laser desorption-ionization mass spectrometry) [36 38]. 

P. Dietemann, M. J. Edelmann, C. Meisterhans, C. Pfeiffer, S. Zumbuhl, R. Knochenmuss, R. Zenobi, Artificial photoaging of triterpenes studied by graphite assisted laser desorption/ ionization mass spectrometry, Helv. Chim. Acta, 3, 1766 1777. 

By employing a laser for the photoionization (not to be confused with laser desorption/ ionization, where a laser is irradiating a surface, see Section 2.1.21) both sensitivity and selectivity are considerably enhanced. In 1970 the first mass spectrometric analysis of laser photoionized molecular species, namely H2, was performed [54]. Two years later selective two-step photoionization was used to ionize mbidium [55]. Multiphoton ionization mass spectrometry (MPI-MS) was demonstrated in the late 1970s [56—58]. The combination of tunable lasers and MS into a multidimensional analysis tool proved to be a very useful way to investigate excitation and dissociation processes, as well as to obtain mass spectrometric data [59-62]. Because of the pulsed nature of most MPI sources TOF analyzers are preferred, but in combination with continuous wave lasers quadrupole analyzers have been utilized [63]. MPI is performed on species already in the gas phase. The analyte delivery system depends on the application and can be, for example, a GC interface, thermal evaporation from a surface, secondary neutrals from a particle impact event (see Section 2.1.18), or molecular beams that are introduced through a spray interface. There is a multitude of different source geometries. 

Z. Takats, I. Cotte-Rodrfguez, N. Talaty, H. Chen, and R. G. Cooks. Direct, Trace Level Detection of Explosives on Ambient Surfaces by Desorption Electrospray Ionization Mass Spectrometry. Chem. Commun., no. 15 (2005) 1950-1952. 

J. Shiea, M.-Z. Huang, H.-J. HSu, C.-Y. Lee, C.-H. Yuan, I. Beech, and J. Sunner. Electrospray-Assisted Laser Desorption/Ionization Mass Spectrometry for Direct Ambient Analysis of Solids. Rapid Commun. Mass Spectrom., 19(2005) 3701-3704. 

J. Wei, J. M. Buriak, and G. Siuzdak. Desorption-Ionization Mass Spectrometry on Porous Silicon. Nature, 399(1999) 243-246. 

M. Karas, U. Bahr, and F. Hillenkamp. UV Laser Desorption/Ionization Mass Spectrometry of Proteins in the 100,000 Dalton Range. Int. J. Mass Spectrom. Ion Proc., 92(1989) 231-242. 

---