Preface. I. Proteomics And Peptidomics.
Blue Native PAGE and mass spectrometry analysis of ephrin stimulation-dependent protein-protein interactions in NG1O8-EphB2 cells; C.C. Dane et al.- Structure, Processing, and Polymerization of Rainbow Trout Egg Vitelline Envelope Proteins; C.C. Dane et al.- MALDI/MS Comparison of Fe-NTA Immobilized Metal Affinity Chromatography and Commercially-Available Metal Oxide Affinity Resins for Phosphopeptide Enrichment; M.B. Gates et al.- Molecular recognition specificity of anti-3-nitrotyrosine antibodies revealed by affinity-mass spectrometry and immunoanalytical methods; B.A. Petre et al.- II. Lipidomics.
Mapping and sequencing of gangliosides from anencephaly by electrospray ionization high capacity ion trap mass spectrometry; C. Mosoarca et al.- III. Glycomics.
Structural analysis of chondroitin sulfate disaccharides by electrospray ionization high capacity ion trap mass spectrometry; A. Muresan et al.- Application of high performance mass spectrometry to structural analysis of glycosaminoglycan oligosaccharides; D.G. Seidler.- Site specific identification of N-linked glycosylation in proteins by liquid chromatography - electrospray ionization tandem mass spectrometry; I. Perdivara et al.- IV. Immunology.
Characterization of lmmune Responses to Pathogen Challenge by MS Based Epitope Mapping; J.G. Williams et al.- Chemical Surface Modification and Chemical Crosslinking Combined with Mass Spectrometry for Protein Tertiary Structural Information; L.J. Deterding and K.B. Tomer.- V. Small Molecules.
Brominated Flame Retardants: Analytical, Toxicological and Environmental Aspects; A. Covaci and A.C. Dirtu.- Stereochemistry studies of some 1,3-dioxane derivatives by differential mass spectrometry and computational chemistry; F. Harja et al.- MALDI-TOF Mass Spectrometry in Textile Industry; F.-D. Munteanu et al.- MALDI MS in Analysis of Keratin Fibre Proteins; A. Körner.-Chemical structure identification by differential mass spectra; N. Dinca.-
List of Contributors.
Mass spectrometry (MS) along with its hyphenated techniques is capable of high throughput, sensitivity, accuracy and selectivity for the analysis of structure and composition of almost any product. Like in electrophoresis, MS separates mo- cules based on the mass-to-charge ratio. In case of gel electrophoresis (SDS- PAGE), a well-known and efficient bioanalytical technique, proteins bear negative charges but have the same charge density, so proteins are separated according to their size. Similarly, in case of MS analysis, proteins carry the same charge, and are separated by their molecular weight. Unlike SDS-PAGE, however, modern ultra high resolution MS discerns very small mass differences and can resolve and completely identify in a single experiment species of the same nominal mass in complex biological mixtures. Consequently, MS can be used for the structural characterization, identification and sensitive detection of mixtures of biomolecules or for assessing the quality of isolated proteins (purity, integrity, or post-translational modifications, for example), carbohydrates, nucleic acids, drugs, metabolites, pollutants etc. In the post-genome era, MS is continuously developing as one of the most re- able analytical method for elucidating the structure of molecules originating from various biological matrices. The potential of MS for high-sensitive structural a- lyses became unsurpassable after the introduction of electrospray (ESI) and matrix assisted laser/desorption ionization (MALDI) methods, on one hand, and the pos- bility to deduce in detail unknown biopolymer structures by highly accurate mo- cular mass measurement followed by sequencing using dissociation techniques based on multiple stage MS, on the other.
Mass spectrometry use to 'Omics'
Mass Ssectrometry for immunology
Mass Spectrometry use for controlling the environment
Mass spectrometry for chemical structure identification