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Matrix-assisted laser desorption/ionization membrane

The two membranes most used for protein work are nitrocellulose and polyvi-nylidene fluoride (PVDF). Both bind proteins at about 100 pg/cm2. Nitrocellulose is the best membrane to use in the initial stages of an experiment. PVDF is used when proteins are to be sequenced or placed into a (matrix-assisted laser desorption ionization) mass spectrometer. PVDF can withstand the harsh chemicals of protein sequenators and the heat generated by mass spectrometer lasers, whereas nitrocellulose cannot. [Pg.152]

J. Guittard, X. P. L. Hronowski, and C. E. Costello, Direct matrix-assisted laser desorption/ ionization mass spectrometric analysis of glycosphingolipids on thin layer chromatographic plates and transfer membranes, Rapid Commun. Mass Spectrom., 13 (1999) 1838-1849. [Pg.137]

Stevenson, T. I. Loo, J. A. Greis, K. D. 1998. Coupling capillary high-performance liquid chromatography to matrix-assisted laser desorption/ionization mass spectrometry and N-terminal sequencing of peptides via automated microblotting onto membrane substrates. Anal. Biochem., 262,99-109. [Pg.227]

Interaction of nanomaterials with native cells is an important problem in modem life science. Recent progress in mass spectrometry provides a vital tool to study this problem. Advances in applications of mass spectrometry for investigating the interaction of nanoparticles with cell membranes and biomacromolecules are based on at least two methods. The first is matrix-assisted laser desorption ionization (MALDI),1 and the second is temperature-programmed desorption mass spectrometry (TPD MS), newly developed to study the interaction of nanoparticles with a cell surface.2 ... [Pg.277]

Low, TY, Seow, TK. and Chung, M.C. (2002) Separation of human erythrocyte membrane associated proteins with one-dimensional and two-dimensional gel electrophoresis followed by identification with matrix-assisted laser desorption/ionization-time of flight mass spectrometry. Proteomics 2,... [Pg.127]

Zhang, H. and Caprioli, R.M. (1996) Capillary electrophoresis combined with matrix-assisted laser desorption/ionization mass spectrometry continous sample deposition on a matrix-precoated membrane target. J. Mass Spectrom. 31, 1039-1046. [Pg.380]

Sample Preparation Using Synthetic Membranes for the Study of Biopolymers By Matrix Assisted Laser Desorption/Ionization Mass Spectrometry... [Pg.143]

In this study, we used matrix-assisted laser desorption ionization /Mass Spectrometry (MALDI/MS) to identify the peptides released from gastric parietal cell microsomes. MALDI, because of its sensitivity and relative tolerance to the presence of salts and buffers was examined for the analysis of unfractionated proteolytic digests (9, 10). MALDI with post-source decay (PSD) analysis was used to obtain sequence information on peptides even in crude digestion mixtures. Our strategy (Figure 1) consisted of proteolysis of intact vesicles, centrifugation at high speeds to separate membrane bound and soluble fractions and analysis of the mixture of released peptides by MALDI/MS. In addition, to increase the... [Pg.533]

Ohtsu, L, Nakanisi, T, Furuta, M., Ando, E., and Nishimura, O., Direct matrix-assisted laser desorption/ionization time-of-flight mass spectrometric identification of proteins on membrane detected by Western blotting and lectin blotting, Journal ofProteome Research, 4, 1391-1396, 2005. [Pg.1367]

Worrall, T. A., Cotter, R. J., and Woods, A. S., Purification of contaminated peptides and proteins on synthetic membrane surfaces for matrix-assisted laser/desorption ionization mass spectrometry. Analytical Chemistry, 70, 750-756, 1998. [Pg.1368]

Nakanishi T, Ohtsu I, Furuta M, Ando E, Nishimura O. Direct MS/MS analysis of proteins blotted on membranes by a matrix-assisted laser desorption/ionization-quadrupole ion trap-time-of-flight tandem mass spectrometer. J Proteome Res 2005 4 743-747. [Pg.480]

Rosinke, B., Strupat, K., Hillenkamp, F., Rosenbusch, J., Dencher, N., KrUger, U., and Galla, H.-J. (1995) Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) of membrane proteins and non-covalent complexes. J. Mass Spectrom., 30, 1462-14. [Pg.37]

J.J. Lu, Z. Zhu, W. Wang, S. Liu, Coupling sodium dodecyl sulfate-capillary polyacrylamide gel electrophoresis with matrix-assisted laser desorption ionization time-of-flight mass spectrometry via a poly(tetrafluoroethylene) membrane. Anal. Chem. 83 (5) (2011) 1784-1790. [Pg.314]

Nevertheless, planar electrophoretic techniques are very popular in biotechnological and biochemical laboratories. There is still no online interface, directly linking such techniques with mass spectrometric detectors. A handful of experiments were described, regarding the identification of proteins transferred onto the membrane after immunoblotting [6,7]. Secondary ion mass spectrometry (SIMS) and matrix-assisted laser desorption/ionization (MALDI) techniques were used for the direct analysis of intact proteins or after sputtering blots with trypsin solution for digestion... [Pg.76]


See other pages where Matrix-assisted laser desorption/ionization membrane is mentioned: [Pg.490]    [Pg.113]    [Pg.167]    [Pg.482]    [Pg.207]    [Pg.241]    [Pg.247]    [Pg.319]    [Pg.97]    [Pg.332]    [Pg.597]    [Pg.2]    [Pg.266]    [Pg.51]    [Pg.476]    [Pg.74]    [Pg.364]    [Pg.3955]    [Pg.104]    [Pg.961]    [Pg.465]   
See also in sourсe #XX -- [ Pg.248 ]




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Assisted Laser Desorption

Desorption ionization

Laser assisted

Laser desorption

Laser ionization

Laser ionizing

Matrix assisted

Matrix assisted desorption+ionization

Matrix assisted laser ionization

Matrix ionization

Matrix-assisted laser

Matrix-assisted laser desorption ionization

Matrix-assisted laser-desorption

Membrane matrix

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