Electrospray Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometry for Lectin Analysis

摘要

Since the introduction of electrospray ionization (ESI) [1, 2] and matrix-assisted laser desorption/ionization (MALDI) [3, 4], these "soft" ionization techniques have dramatically changed the field of mass spectrometry. ESI and MALDI allow for the ionization of large non-volatile molecules, while yielding little or no fragmentation. They are applicable to a wide variety of molecules, ranging from peptides, proteins, oligonucleotides, oligosaccharides, and polymers, to lipids. These techniques are also suitable for extremely large molecules, rendering mass determination of species larger than 100,000 Da feasible. Currently, ESI and MALDI are the most commonly used ionization techniques for mass spectrometric analysis of biomolecules. Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) was introduced in 1974 by Comisarow and Marshall [5], and since its inception has proven itself to be a valuable tool for the characterization of biomolecules. The employment of FT-ICR MS for biomolecular structural characterization offers several advantages, including high mass resolution, ultrahigh mass accuracy, and a wide mass range. FT-ICR MS is also an extremely versatile technique, and is capable of performing several varieties of tandem mass spectrometric methods (see Section 6) [6-11].