Matrix-assisted laser-desorption ionization mass mapping

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Wang, Q. Jakubowski, J. A. Sweedier, J. V. Bohn, P. W., Quantitative submonolayer spatial mapping of Arg-Gly-Asp-containing peptide organo-mercaptan gradients on gold with matrix-assisted laser desorption/ionization mass spectrometry, Anal. Chem. 2004, 76, 1-8... [Pg.80]

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Figure 8 Scheme for differential labeling of two samples with do/da acrylamide (alkylation of Cys residues). The central map refers to rat sera, labeled separately with either do- or ds-acrylamide and mixed in a 30 70% ratio. (Reproduced from Gehanne S, Cecconi D, Carbon L, et al. (2002) Quantitative analysis of two-dimensional gel-separated proteins using isotopically marked alkylating agents and matrix-assisted laser desorption/ionization mass spectrometry. Reipid Communications in Mass Spectrometry 16 1692-1698.)... [Pg.1003]

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Today, two-dimensional mass spectrometry analysis of biological tissues by means of a technique called mass imaging, mass spectrometry imaging (MSI), or imaging mass spectrometry has been used in mapping the distribution of elements or chemical groups in samples. Matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS), secondary ion mass spectrometry (SIMS), and laser ablation inductively coupled plasma mass spectrometry (LA-ICP-MS) are three commonly used MSI techniques. [Pg.328]

Billeci, T. Stults, J. Tryptic mapping of recombinant proteins by matrix-assisted laser desorption/ionization mass spectrometry. Anal Chem. 1993,65,1709-1718. [Pg.241]

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Matrix-assisted laser desorption-ionization ionizes molecules with molecular masses of 100-1,000,000 Da for analysis by MS and provides high sensitivity, high throughput, and simplicity of operation. MALDI combined with enzymatic reactions and protein chemistry can provide very useful information on molecular masses, peptide maps, and primary structure.15 MALDI-TOF MS can quickly and accurately determine unfractionated mixtures at concentrations below 100 fmol per liter. The obtained data are then calibrated with internal standards, monoisotopic masses are assigned for all prominent peaks, and the peptide list thus generated is used to identify the protein by using a suitable database.16... [Pg.698]

Biological materials often contain proteins that must be identified. Recent advances in mass spectrometry have made peptide mapping a convenient tool for this purpose. The protein in question is selectively hydrolyzed with a peptidase such as trypsin and the mixture of peptides produced is analyzed by matrix-assisted laser desorption ionization (MALDI) as illustrated in Figure 25.10. [Pg.1146]

Troendle, F.J. A quadrupole ion trap laser microprobe for the mapping of pharmaceutical compounds in intact tissue. Ph.D. Dissertation, University of Florida, 2000. Troendle, F.J. Reddick, C.D. Yost, R.A. Detection of pharmaceutical compounds in tissue by matrix-assisted laser desorption/ ionization and laser desorption/chemical ionization tandem mass spectrometry with a quadrupole ion trap. J. Am. Soc. Mass Spectrom. 1999,10, 1315-1321. [Pg.437]