LC coupled to ESI, MALDI and ICP MS - A multiple hyphenation for metalloproteomic studies

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Publikace nespadá pod Fakultu sportovních studií, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.
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COUFALÍKOVÁ Kateřina BENEŠOVÁ Iva VACULOVIČ Tomáš KANICKÝ Viktor PREISLER Jan

Rok publikování 2017
Druh Článek v odborném periodiku
Časopis / Zdroj Analytica Chimica Acta
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
Doi http://dx.doi.org/10.1016/j.aca.2017.03.016
Obor Analytická chemie, separace
Klíčová slova Matrix-assisted laser desorption/ionization; mass spectrometry; Inductively coupled plasma mass; spectrometry; Electrospray ionization mass spectrometry; Liquid chromatography; Metallothionein isoforms; Metal complexes
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. (C) 2017 Elsevier B.V. All rights reserved.
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