Detailed Information on Publication Record
2017
LC coupled to ESI, MALDI and ICP MS - A multiple hyphenation for metalloproteomic studies
COUFALÍKOVÁ, Kateřina, Iva BENEŠOVÁ, Tomáš VACULOVIČ, Viktor KANICKÝ, Jan PREISLER et. al.Basic information
Original name
LC coupled to ESI, MALDI and ICP MS - A multiple hyphenation for metalloproteomic studies
Authors
COUFALÍKOVÁ, Kateřina (203 Czech Republic, belonging to the institution), Iva BENEŠOVÁ (203 Czech Republic, belonging to the institution), Tomáš VACULOVIČ (203 Czech Republic, belonging to the institution), Viktor KANICKÝ (203 Czech Republic, belonging to the institution) and Jan PREISLER (203 Czech Republic, guarantor, belonging to the institution)
Edition
Analytica Chimica Acta, Amsterdam, Elsevier Science BV, 2017, 0003-2670
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10406 Analytical chemistry
Country of publisher
Netherlands
Confidentiality degree
není předmětem státního či obchodního tajemství
Impact factor
Impact factor: 5.123
RIV identification code
RIV/00216224:14310/17:00094859
Organization unit
Faculty of Science
UT WoS
000398436800006
Keywords in English
Matrix-assisted laser desorption/ionization; mass spectrometry; Inductively coupled plasma mass; spectrometry; Electrospray ionization mass spectrometry; Liquid chromatography; Metallothionein isoforms; Metal complexes
Změněno: 6/4/2018 11:38, Ing. Nicole Zrilić
Abstract
V originále
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.
Links
| GA15-05387S, research and development project |
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| LQ1601, research and development project |
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