Ionization biological mass spectrometry

Morris, H.R. (1980) Soft Ionization Biological Mass Spectrometry, Heyden, London. 

Hunt, D.F., Buko, A.M., Ballard, J.M., Shabanowitz, J. and Giordani, A.B. (1980) Sequence analysis of polypeptides by collision activated dissociation on a triple quadrupole mass spectrometer. In Soft Ionization Biological Mass Spectrometry. H. Morris, ed. (London Heyden Sons Ltd.), pp. 85-109. 

Schulterr, H.-R., Advances in field desorption mass spectrometry, in Soft Ionization Biological Mass Spectrometry, Morris, H. R., Ed., Heyden, London, 1981, p. 6. Wood, G. W., Field desorption mass spectrometry Applications, Mass Spectrom. 

R.D. Smith, K.J. Light-Wahl, B.E. Winger and D.R. Goodlett, Electrospray ionization. In T. Matsuo, R.M. Caprioli, M.L. Gross and Y. Seyama (Eds.), Biological Mass Spectrometry Present and Future, Wiley, New York, 1994, pp. 41-74. 

This proposal describes the development of a new, systematic approach for qualitatively and quantitatively studying surface-biomolecule interactions by matrix-assisted laser desorption ionization (MALDl) mass spectrometry (MS). This methodology is being developed because of the profound importance that surface-biomolecule interactions play in applications where biomaterials come into contact with complex biological fluids, it can readily be shown that undesired reactions occurring in response to surface-biomolecule contact (protein adsorption, biofouling, immune response activation, etc.) lead to enormous economic and human costs. Thus, the development of analytical methodologies that allow for efficient assessment of the properties of new biomaterials and/or the study of detailed fundamental processes initiated upon surface-biomolecule contact are of critical value ... 

Volmer D.A., B. Mansoori, and S.J. Locke (1997). Study of 4-quinolone antibiotics in biological samples by short-column liquid chromatography coupled with electrospray ionization tandem mass spectrometry. Analytical Chemistry 69 4143 155. 

Hillenkamp, F., Karas, M., Ingeldoh, A. and Stahl, B. (1990) Matrix assisted UV-laser desorption ionization a new approach to mass spectrometry of large molecules, in Biological Mass Spectrometry, p. 49 (eds A.L. Burlingame and J.A. McCloskey), Elsevier, Amsterdam. 

Brtigger B, Erben G, Sandhoff R, Wieland FT, Lehmann WD. Quantitative analysis of biological membrane lipids at the low picomole level by nano electrospray ionization tandem mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 1997 94 2339-2344. 

Han X. Characterization and direct quantitation of ceramide molecular species from lipid extracts of biological samples by electrospray ionization tandem mass spectrometry. Anal. Biochem 2002 302 199-212. 

Kaufmann, R. Matrix-assisted laser desorption ionization (MALDI) mass spectrometry A novel anal3dical tool in molecular biology and biotechnology. J. Biotechnol. 1995, 41, 155-175. 

Naylor S, Johnson KL, Williamson BL, Klarskov K, and Gleich GJ (1999) Structural characterization of contaminants in commercial preparations of melatonin by on-line HPLG-electrospray ionization-tandem mass spectrometry. Advances in Experimental Medicine and Biology 467 769-777. 

For reviews of ionization of neutral fragments as a structural probe see (a) MJ Polce, S Beranova, MJ Nold, C Wesdemiotis. Characterization of neutral fragments in tandem mass spectrometry a unique route to mechanistic and structural information. J Mass Spectrom 31 1073—1085,1996 (b) MM Cordero, C Wesdemiotis, Reionization and characterization of neutral losses from biomolecular ions. In Biological Mass Spectrometry Present and Future. New York Wiley, 1994, pp 119—126. 

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 2.5. Schematic diagram of plasma desorption ionization and time-of-flight mass spectrometry. (Reproduced from C. Dass, Principles and Practice of Biological Mass Spectrometry, Wiley-Interscience, 2001.)...

Figure 3.13. Principle of an orthogonal time-of-flight mass analyze. A beam of ions from a continuons ionization source, such as ESI, are transmitted between the orthogonal ion extraction plate and grid. A segment of the beam is then pushed into the field-free region by a pulse in the orthogonal direction. (Reproduced from C. Dass, Principles and Practice of Biological Mass Spectrometry, WUey-lntescience, 2001.)...

Yu-Chie Chen received her education from the National Sun Yat-Sen University (MSc) and Montana State University (PhD). She is Professor of Chemistry at the National Chiao Tung University. Her research interests include biological mass spectrometry, nanomedicine, and nanotechnology. She is the co-inventor of several ionization techniques for mass spectrometry (SAUDI, UASI, C-API, PI-ESI), which are useful in the monitoring of chemical reactions. 

Yi-Sheng Wang received his education from the Feng Chia University (BEng) and the National Taiwan University (PhD). He is currently Associate Research Fellow in the Genomics Research Center of Academia Sinica. His research covers in-depth developments in mass spectfometry instrumentation, fundamental research on ionization chemistry, method development and applications of biological mass spectrometry. 

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