LC coupled to ESI, MALDI and ICP MS - A multiple hyphenation for metalloproteomic studies
| Autor: | Tomáš Vaculovič, Jan Preisler, Kateřina Coufalíková, Viktor Kanický, Iva Benešová |
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| Rok vydání: | 2016 |
| Předmět: |
MALDI imaging
Proteomics Spectrometry Mass Electrospray Ionization Protein mass spectrometry Electrospray ionization Analytical chemistry 010402 general chemistry Mass spectrometry 01 natural sciences Biochemistry Sample preparation in mass spectrometry Analytical Chemistry Environmental Chemistry Direct electron ionization liquid chromatography–mass spectrometry interface Inductively coupled plasma mass spectrometry Spectroscopy Chromatography Chemistry Lasers 010401 analytical chemistry 0104 chemical sciences Matrix-assisted laser desorption/ionization Metals Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Metallothionein Chromatography Liquid |
| Zdroj: | Analytica chimica acta. 968 |
| ISSN: | 1873-4324 |
| Popis: | A new multiple detection arrangement for liquid chromatography (LC) that supplements conventional electrospray ionization (ESI) mass spectrometry (MS) detection with two complementary detection techniques, matrix-assisted laser desorption/ionization (MALDI) MS and substrate-assisted laser desorption inductively coupled plasma (SALD ICP) MS has been developed. The combination of the molecular and elemental detectors in a single separation run is accomplished by utilizing a commercial MALDI target made of conductive plastic. The proposed platform provides a number of benefits in today's metalloproteomic applications, which are demonstrated by analysis of a metallothionein mixture. To maintain metallothionein complexes, separation is carried out at a neutral pH. The effluent is split; a major portion is directed to ESI MS while the remaining 1.8% fraction is deposited onto a plastic MALDI target. Dried droplets are overlaid with MALDI matrix and analysed consecutively by MALDI MS and SALD ICP MS. In the ESI MS spectra, the MT isoform complexes with metals and their stoichiometry are determined; the apoforms are revealed in the MALDI MS spectra. Quantitative determination of metallothionein isoforms is performed via determination of metals in the complexes of the individual protein isoforms using SALD ICP MS. |
| Databáze: | OpenAIRE |
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