Complementary MALDI MS and SALD ICP MS detection of a single
separation record for metalloprotein analaysis

a 2013

Complementary MALDI MS and SALD ICP MS detection of a single separation record for metalloprotein analaysis

TOMALOVÁ, Iva; Pavla FOLTYNOVÁ; Viktor KANICKÝ a Jan PREISLER

Základní údaje

Originální název

Complementary MALDI MS and SALD ICP MS detection of a single separation record for metalloprotein analaysis

Autoři

TOMALOVÁ, Iva (203 Česká republika, domácí); Pavla FOLTYNOVÁ (203 Česká republika, domácí); Viktor KANICKÝ (203 Česká republika, domácí) a Jan PREISLER (203 Česká republika, garant, domácí)

Vydání

3. Konference České společnosti pro hmotnostní spektrometrii, 2013

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10406 Analytical chemistry

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Kód RIV

RIV/00216224:14740/13:00066467

Organizační jednotka

Středoevropský technologický institut

ISBN

978-80-905045-3-0

Klíčová slova anglicky

metalloproteomics; MALDI TOF MS; SALD ICP MS; separation

Změněno: 12. 12. 2013 14:25, Mgr. Iva Benešová, Ph.D.

Anotace

V originále

Metals play a crucial role in physiology and pathology of biological systems. It has been estimated that the metalloproteins encompass about one third of all proteins. A novel method for comprehensive multidimensional analysis of metalloproteins is presented here. This approach is based on an off-line coupling of a single micro-column separation run to both substrate-assisted laser desorption (SALD) inductively coupled plasma (ICP) mass spectrometry (MS) and matrix-assisted laser desorption/ionization mass spectrometry (MALDI) MS. The effluent fractions are collected on a custom-designed Au-coated polyethylene terephthalate glycol (PETG) sample target that is compatible to both MS methods. The whole concept is demonstrated on analysis of rabbit-liver metallothionein (MT) isoform mixture. The MTs are separated by capillary electrophoresis (CE) coupled to MALDI MS/SALD ICP MS via a liquid junction interface and a sub-atmospheric deposition chamber. MALDI MS and SALD ICP MS provide information about both molecular mass of present proteins and metal distribution and quantity, respectively. We believe the presented method is a viable alternative to on-line coupling employing electrospray ionization and nebulizer ICP MS. The off-line hyphenation allows decoupling separation and both detection processes in time and space and offers further options, e.g. re-analysis or archiving of the separation record, laser-induced fluorescence detection or on target protein digestion.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

GAP206/12/0538, projekt VaV

Název: Nové strategie úpravy vzorků pro desorpční hmotnostní spektrometrii

Investor: Grantová agentura ČR, Nové strategie úpravy vzorků pro desorpční hmotnostní spektrometrii

Citovat

TOMALOVÁ, Iva; Pavla FOLTYNOVÁ; Viktor KANICKÝ a Jan PREISLER. Complementary MALDI MS and SALD ICP MS detection of a single separation record for metalloprotein analaysis. In 3. Konference České společnosti pro hmotnostní spektrometrii. 2013. ISBN 978-80-905045-3-0.

@proceedings{1127499,
   author = {Tomalová, Iva and Foltynová, Pavla and Kanický, Viktor and Preisler, Jan},
   booktitle = {3. Konference České společnosti pro hmotnostní spektrometrii},
   keywords = {metalloproteomics; MALDI TOF MS; SALD ICP MS; separation},
   language = {eng},
   isbn = {978-80-905045-3-0},
   title = {Complementary MALDI MS and SALD ICP MS detection of a single separation record for metalloprotein analaysis},
   year = {2013}
}

TY  - CONF
ID  - 1127499
AU  - Tomalová, Iva - Foltynová, Pavla - Kanický, Viktor - Preisler, Jan
PY  - 2013
TI  - Complementary MALDI MS and SALD ICP MS detection of a single separation record for metalloprotein analaysis
SN  - 9788090504530
KW  - metalloproteomics
KW  - MALDI TOF MS
KW  - SALD ICP MS
KW  - separation
N2  - Metals play a crucial role in physiology and pathology of biological systems. It has been estimated that the metalloproteins encompass about one third of all proteins. A novel method for comprehensive multidimensional analysis of metalloproteins is presented here. This approach is based on an off-line coupling of a single micro-column separation run to both substrate-assisted laser desorption (SALD) inductively coupled plasma (ICP) mass spectrometry (MS) and matrix-assisted laser desorption/ionization mass spectrometry (MALDI) MS. The effluent fractions are collected on a custom-designed Au-coated polyethylene terephthalate glycol (PETG) sample target that is compatible to both MS methods. The whole concept is demonstrated on analysis of rabbit-liver metallothionein (MT) isoform mixture. The MTs are separated by capillary electrophoresis (CE) coupled to MALDI MS/SALD ICP MS via a liquid junction interface and a sub-atmospheric deposition chamber. MALDI MS and SALD ICP MS provide information about both molecular mass of present proteins and metal distribution and quantity, respectively. We believe the presented method is a viable alternative to on-line coupling employing electrospray ionization and nebulizer ICP MS. The off-line hyphenation allows decoupling separation and both detection processes in time and space and offers further options, e.g. re-analysis or archiving of the separation record, laser-induced fluorescence detection or on target protein digestion.
ER  -

TOMALOVÁ, Iva; Pavla FOLTYNOVÁ; Viktor KANICKÝ a Jan PREISLER. Complementary MALDI MS and SALD ICP MS detection of a single separation record for metalloprotein analaysis. In \textit{3. Konference České společnosti pro hmotnostní spektrometrii}. 2013. ISBN~978-80-905045-3-0.

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