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Myoglobin mass spectrometry

Bolton, J. L. Le Blanc, J. C. Y. Siu, K. W. M. Reaction of quinone methides with proteins analysis of myoglobin adduct formation by electrospray mass spectrometry. Biol. Mass... [Pg.352]

Figure 2.9. Schematic of a matrix-assisted laser desorption/ionization (MALDI) event. The SEM micrograph depicts sinapinic acid-equine myoglobin crystal from a sample prepared according to the dried drop sample preparation method. In the desorption event neutral matrix molecules (M), positive matrix ions (M+), negative matrix ions (M-), neutral analyte molecules (N), positive analyte ions (+), and negative analyte ions (-) are created and/or transferred to the gas phase. Reprinted from A. Westman-Brinkmalm and G. Brinkmalm (2002). In Mass Spectrometry and Hyphenated Techniques in Neuropeptide Research, J. Silberring and R. Ekman (eds.) New York John Wiley Sons, 47-105. With permission of John Wiley Sons, Inc. Figure 2.9. Schematic of a matrix-assisted laser desorption/ionization (MALDI) event. The SEM micrograph depicts sinapinic acid-equine myoglobin crystal from a sample prepared according to the dried drop sample preparation method. In the desorption event neutral matrix molecules (M), positive matrix ions (M+), negative matrix ions (M-), neutral analyte molecules (N), positive analyte ions (+), and negative analyte ions (-) are created and/or transferred to the gas phase. Reprinted from A. Westman-Brinkmalm and G. Brinkmalm (2002). In Mass Spectrometry and Hyphenated Techniques in Neuropeptide Research, J. Silberring and R. Ekman (eds.) New York John Wiley Sons, 47-105. With permission of John Wiley Sons, Inc.
Some reviews [5-7] have appeared on NCE-electrospray ionization-mass spectrometry (NCE-ESI-MS) discussing various factors responsible for detection. Recently, Zamfir [8] reviewed sheathless interfacing in NCE-ESI-MS in which the authors discussed several issues related to sheathless interfaces. Feustel et al. [9] attempted to couple mass spectrometry with microfluidic devices in 1994. Other developments in mass spectroscopy have been made by different workers. McGruer and Karger [10] successfully interfaced a microchip with an electrospray mass spectrometer and achieved detection limits lower than 6x 10-8 mole for myoglobin. Ramsey and Ramsey [11] developed electrospray from small channels etched on glass planar substrates and tested its successful application in an ion trap mass spectrometer for tetrabutylammonium iodide as model compound. Desai et al. [12] reported an electrospray microdevice with an integrated particle filter on silicon nitride. [Pg.92]

C. F. Harrington, S. Elahi, S. A. Merson, P. Ponnampalavanar, Quantitative analysis of iron-containing protein myoglobin in different foodstuffs by liquid chromatography coupled to high-resolution inductively coupled plasma mass spectrometry, J. AOAC Int., 87 (2004), 253 D258. [Pg.532]

In this respect, the paper of Zaia et al. [29], entitled ""The correct molecular weight of myoglobin, a common calibrant for mass spectrometry", is also of interest. It shows that the correct average molecnlar mass of horse heart myoglobin is 16,951.49 Da rather than freqnently given 16,950.5 Da. [Pg.32]

Simmons, D.A., Dunn, S.D., Konermann, L. (2003) Conformational dyneunics of partially denatured myoglobin studied by time-resolved electrospray mass spectrometry with online hydrogen-deuterium exchange. Biochemistry, 42 (19), 5896-5905. [Pg.89]

Buijs, J., Ramstrom, M., Danfelter, M., et al. (2003) Localized changes in the structural stability of myoglobin upon adsorption onto silica particles, as studied with hydrogen/deuterium exchange mass spectrometry. J Colloid Interface Sci, 263 (2), 441-448. [Pg.275]

Sophocleous, A.M., Zhang, J., Topp, E.M. (2012) Localized hydration in lyophOized myoglobin by hydrogen-deuterium exchange mass spectrometry. 1. Exchange mapping. Mol Pharm, 9 (4), 718-726. [Pg.276]

Hydrogen Exchange Mass Spectrometry of Membrane Proteins 281 16.2.2 Myoglobin-Vesicle Interaction... [Pg.281]

Figure 2.19. ESI mass spectrum of horse heart myoglobin. (Reproduced from C. Dass, Principles and Practice of Biological Mass Spectrometry, Wiley-Interscience, 2001.)... Figure 2.19. ESI mass spectrum of horse heart myoglobin. (Reproduced from C. Dass, Principles and Practice of Biological Mass Spectrometry, Wiley-Interscience, 2001.)...
D. A. Simmons and L. Konermann, Characterization of transient protein folding intermediates during myoglobin reconstitution by time-resolved electrospray mass spectrometry with on-hne isotope-pulse labeling. Biochemistry 42, 1906-1914 (2002). [Pg.395]

FIGURE 19.6 Representative chromatograms for a myoglobin tryptic peptide, LFTGHPETLEK, obtained from (a) human plasma blank and (b) myoglobin spiked in human plasma, and for a somatropin tryptic peptide, LFDNAMLR, obtained from (c) human plasma blank and (d) somatropin spiked in human plasma. [Figure (a) and (c) reprinted from Li et al. (2009) with permission of Rapid Communication Mass Spectrometry.]... [Pg.624]

Mayr BM, Kohlbacher O, Reinert K, Sturm M, Gropl C, Lange E, Klein C, Huber CG. Absolute myoglobin quantitation in serum by combining two-dimensional liquid chromatography electrospray ionization mass spectrometry and novel data analysis algorithms. J Proteome Res 2006 5(2) 414—421. [Pg.643]

Konermann, L Rosell, F.I., Mauk, A.G., Douglas, D.J. (1997) Acid-induced Denat-uration of Myoglobin Studied by Time-resolved Electrospray Ionization Mass Spectrometry. Biochemistry 36 6448-6454. [Pg.142]

Sogbein, O.O., Simmons, D.A., Konermann, L. (2000) Effects of pH on the Kinetic Reaction Mechanism of Myoglobin Unfolding Studied by Time-resolved Electrospray Ionization Mass Spectrometry. J. Am. Soc. Mass Spectrom. 11 312-319. [Pg.143]

Cammarata, M., Lin, K.-Y, Pruet, J., Liu, H., Brodbelt, J. (2014) Probing the Unfolding of Myoglobin and Domain C of PARP-1 with Covalent Labeling and Top-Down Ultraviolet Photodissociation Mass Spectrometry. Anal. Chem. 86 2534-2542. [Pg.313]

Myoglobin peptides [146] Marine muscle tissue protein, probably of seal species Alaskan pottery fragment, 1200-1400 A.D. NanoESI operating in positive-ion mode, hybrid quadrupole FT-ICR operating in single and tandem mass spectrometry... [Pg.814]


See other pages where Myoglobin mass spectrometry is mentioned: [Pg.435]    [Pg.310]    [Pg.346]    [Pg.873]    [Pg.479]    [Pg.59]    [Pg.346]    [Pg.430]    [Pg.498]    [Pg.99]    [Pg.293]    [Pg.169]    [Pg.74]    [Pg.126]    [Pg.152]    [Pg.267]    [Pg.266]    [Pg.124]   


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