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

Investor logo

Warning

This publication doesn't include Faculty of Sports Studies. It includes Faculty of Science. Official publication website can be found on muni.cz.
Authors

COUFALÍKOVÁ Kateřina BENEŠOVÁ Iva VACULOVIČ Tomáš KANICKÝ Viktor PREISLER Jan

Year of publication 2017
Type Article in Periodical
Magazine / Source Analytica Chimica Acta
MU Faculty or unit

Faculty of Science

Citation
Doi http://dx.doi.org/10.1016/j.aca.2017.03.016
Field Analytic chemistry
Keywords Matrix-assisted laser desorption/ionization; mass spectrometry; Inductively coupled plasma mass; spectrometry; Electrospray ionization mass spectrometry; Liquid chromatography; Metallothionein isoforms; Metal complexes
Description 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.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.

More info