Ionization methods, mass matrix-assisted laser

See alsa Drug Metabolism Metabolite Isolation and Identification Isotope Studies. Liquid Chromatography Liquid Chromatography-Mass Spectrometry. Mass Spectrometry Ionization Methods Overview Matrix-Assisted Laser Desorption Ionization Mass Separation ... [Pg.2811]

Most biochemical analyses by MS use either electrospray ionization (ESI) or matrix-assisted laser desorption ionization (MALD1), typically linked to a time-of-flight (TOF) mass analyzer. Both ESI and MALDl are "soft" ionization methods that produce charged molecules with little fragmentation, even with biological samples of very high molecular weight. [Pg.417]

Mass spectrometry has been revolutionalized by the advent of electrospray ionization, but, before we concentrate on this relatively recent addition to the array of ionization methods, we will first discuss two other techniques which are routinely used for the ionization of biomolecules matrix assisted laser desorption ionization (MALDI) and fast atom bombardment (FAB). These techniques share common features in that ... [Pg.125]

With the identities and amounts of amino acids known, the peptide is seiiuenced to find out in what ordei the amino acids are linked together. Much peptide sequencing is now done by mass spectrometry, using either electrospray ionization (liSi) or matrix-assisted laser desorption ionization (M.ALDI) linked tcr a time-of-flight (TO -) mass analyzer, as described in Section 12.4. Also in common use is a chemical method of peptide sequencing called the Edman degradation. [Pg.1031]

The cornucopia of ionization methods [electron impact ionization (El), chemical ionization (Cl), field desorption (FD), fast atom bombardment (FAB), electrospray ionization (ESI), and matrix-assisted laser desorption/ionization (MALDI)] yield gas-phase ions for mass analysis via quite different physical and chemical processes. Unfortunately, many of these processes are still not well understood. [Pg.86]

T. Yamagaki, Y. Ishizuka, S.-I. Kawahara, H. Nakanishi. Analysis of glycosidic linkages in saccharide compounds by post-source decay fragment methods in matrix-assisted laser desorption/ionization time-of-flight mass spectroscopy. Rap. Comm. Mass. Spec. 1999, /1,527-531. [Pg.316]

See also Carbohydrates Overview. Elemental Speciation Overview. Food and Nutritional Analysis Overview. Gas Chromatography Mass Spectrometry. Lipids Overview. Liquid Chromatography Liquid Chromatography-Mass Spectrometry Food Applications. Mass Spectrometry Overview Principles Ionization Methods Overview Atmospheric Pressure Ionization Techniques Eiectrospray Matrix-Assisted Laser Desorption/lonization Pyrolysis. Proteins Traditional Methods of Sequence Determination. Vitamins Overview. [Pg.2933]

See also Mass Spectrometry Ionization Methods Overview Atmospheric Pressure Ionization Techniques Electrospray Matrix-Assisted Laser Desorption/lonization Time-of-Fiight. Proteins Traditionai Methods of Sequence Determination. Proteomics. [Pg.2961]

Mass spectrometry (MS) in its different detection modes is now the ultimate method for the characterization of the mass, composition, and sequence of peptide or protein components in a mixture and is particularly well suited to the mobile phases employed in RPC. Electrospray ionization (ESI) and matrix-assisted laser desorption ionization time-of-fiight (MALDl-TOF) mass spectroscopic methods, and to a lesser extent thermospray and fast atom bombardment... [Pg.204]

Because of the advances in the gas-phase ionization of biomacromolecules, such as electrospray ionization (ESI) and matrix-assisted laser desorption ionization (MALDI), mass spectrometry (MS) has become a powerful tool for detection, identification, and structural analysis of proteins, peptides, and polynucleotides. The molecules ionized in a gas phase by these methods are subsequently analyzed by sector, quadrupole, ion-trap, or time-of-flight mass spectrometers. In particular, the MS systems consisting of ESI and triple-stage quadrupole (ESI/TSQ) or ion-trap (IT) mass spectrometry and MALDI time-of-flight (MALDl/TOF) mass spectrometry have been most widely applied to the field of protein chemistry for the accurate determination of molecular mass of proteins and peptides, determination of amino acid sequence, identification of proteins by peptide mass databases, and analysis of posttranslational modifications such as phosphorylation and glycosylation. In general, current techniques allow detenni-... [Pg.646]

Sehumaker S, Borror CM, Sandrin TR. Automating data acquisition aifects mass spectrum quality and reproducibility during bacterial profiling using an intact cell sample preparation method with matrix-assisted laser desorption/ionization time-of- light mass speetrometry. Rapid Com-mun Mass Sp. 2012 26(3) 243-53. [Pg.178]