A Multidetection Platform for Proteome Analysis

A 2008

A Multidetection Platform for Proteome Analysis

PREISLER, Jan; Ondřej PEŠ; Pavla FOLTYNOVÁ; Tomáš VACULOVIČ; Pavel KRÁSENSKÝ et. al.

Základní údaje

Originální název

A Multidetection Platform for Proteome Analysis

Název česky

Multidetekční platforma pro výzkum proteomu

Autoři

PREISLER, Jan; Ondřej PEŠ; Pavla FOLTYNOVÁ; Tomáš VACULOVIČ; Pavel KRÁSENSKÝ; Viktor KANICKÝ a Radek VYHNÁNEK

Vydání

Innsbruck, Austria, 8th Csaba Horváth Medal Award Symposium, 2008

Nakladatel

University of Innsbruck

Další údaje

Jazyk

angličtina

Typ výsledku

Audiovizuální tvorba

Obor

10406 Analytical chemistry

Stát vydavatele

Rakousko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL, URL

Kód RIV

RIV/00216224:14310/08:00026591

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

off-line coupling; capillary electrophoresis; mass spectrometry; MALDI; ICP; LIF; proteins

Štítky

Capillary electrophoresis, ICP, LIF, MALDI, mass spectrometry, off-line coupling, proteins

Příznaky

Mezinárodní význam

Změněno: 9. 4. 2013 12:44, prof. Mgr. Jan Preisler, Ph.D.

Anotace

ORIG CZ

V originále

An instrumentation platform based on a universal interface for deposition of CE or microLC eluent on a target of a MALDI mass spectrometer will be described. The deposited fractions of proteins or peptides may be analyzed in off-line mode using MALDI mass or tandem mass spectrometry (MS or MS/MS) and native laser-induced fluorescence (LIF) detection or subjected to on-target reactions, such as digestion for protein identification. An additional detection mode is inductively coupled plasma mass spectrometry (ICP MS), nature of which is complementary to soft MALDI MS. We propose substrate assisted laser desorption (SALD) of sample from the target and sample transfer to ICP. Thus, both information about protein identity and content of elements, such as metals or phosphorus are available from a single separation record. Using the platform, sub-picomolar quantities of proteins are detected, digested and identified directly on MALDI target. LIF detection of protein bands is found to be sensitive, fast and generally useful for tryptophan-containing proteins. Although not as sensitive as the on-column LIF detection, on-target LIF detection may be used to select fractions containing proteins. Consequently on-target peptide mass fingerprinting is carried out to identify protein in the selected fractions. For the SALD ICP MS detection, influence of desorption laser fluence, presence of additives or role of substrate is discussed. Selected metals are detected in sub-picomolar amounts. MALD-ICP MS analysis of chromium species (Cr3+ and CrO42-) will be shown to demonstrate the coupling for metal analysis. High separation efficiency is maintained due to the employed liquid junction and fraction deposition.

Česky

Viz anglický abstrakt

Návaznosti

LC06035, projekt VaV

Název: Centrum biofyzikální chemie, bioelektrochemie a bioanalýzy. Nové nástroje pro genomiku, proteomiku a biomedicínu.

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Centrum biofyzikální chemie, bioelektrochemie a bioanalýzy. Nové nástroje pro genomiku, proteomiku a biomedicínu

MSM0021622415, záměr

Název: Molekulární podstata buněčných a tkáňových regulací

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Molekulární podstata buněčných a tkáňových regulací

Citovat

PREISLER, Jan; Ondřej PEŠ; Pavla FOLTYNOVÁ; Tomáš VACULOVIČ; Pavel KRÁSENSKÝ; Viktor KANICKÝ a Radek VYHNÁNEK. A Multidetection Platform for Proteome Analysis. Innsbruck, Austria: University of Innsbruck, 2008. 8th Csaba Horváth Medal Award Symposium.

@misc{786605,
   author = {Preisler, Jan and Peš, Ondřej and Foltynová, Pavla and Vaculovič, Tomáš and Krásenský, Pavel and Kanický, Viktor and Vyhnánek, Radek},
   address = {Innsbruck, Austria},
   keywords = {off-line coupling; capillary electrophoresis; mass spectrometry; MALDI; ICP; LIF; proteins},
   language = {eng},
   location = {Innsbruck, Austria},
   publisher = {University of Innsbruck},
   title = {A Multidetection Platform for Proteome Analysis},
   url = {http://congressinfo.net/horvath8/},
   year = {2008}
}

TY  - GEN
ID  - 786605
AU  - Preisler, Jan - Peš, Ondřej - Foltynová, Pavla - Vaculovič, Tomáš - Krásenský, Pavel - Kanický, Viktor - Vyhnánek, Radek
PY  - 2008
TI  - A Multidetection Platform for Proteome Analysis
VL  - 8th Csaba Horváth Medal Award Symposium
PB  - University of Innsbruck
CY  - Innsbruck, Austria
KW  - off-line coupling
KW  - capillary electrophoresis
KW  - mass spectrometry
KW  - MALDI
KW  - ICP
KW  - LIF
KW  - proteins
UR  - http://congressinfo.net/horvath8/
L2  - http://congressinfo.net/horvath8/
N2  - An instrumentation platform based on a universal interface for deposition of CE or microLC eluent on a target of a MALDI mass spectrometer will be described. The deposited fractions of proteins or peptides may be analyzed in off-line mode using MALDI mass or tandem mass spectrometry (MS or MS/MS) and native laser-induced fluorescence (LIF) detection or subjected to on-target reactions, such as digestion for protein identification. An additional detection mode is inductively coupled plasma mass spectrometry (ICP MS), nature of which is complementary to soft MALDI MS. We propose substrate assisted laser desorption (SALD) of sample from the target and sample transfer to ICP. Thus, both information about protein identity and content of elements, such as metals or phosphorus are available from a single separation record. Using the platform, sub-picomolar quantities of proteins are detected, digested and identified directly on MALDI target. LIF detection of protein bands is found to be sensitive, fast and generally useful for tryptophan-containing proteins. Although not as sensitive as the on-column LIF detection, on-target LIF detection may be used to select fractions containing proteins. Consequently on-target peptide mass fingerprinting is carried out to identify protein in the selected fractions. For the SALD ICP MS detection, influence of desorption laser fluence, presence of additives or role of substrate is discussed. Selected metals are detected in sub-picomolar amounts. MALD-ICP MS analysis of chromium species (Cr3+ and CrO42-) will be shown to demonstrate the coupling for metal analysis. High separation efficiency is maintained due to the employed liquid junction and fraction deposition.
ER  -

PREISLER, Jan; Ondřej PEŠ; Pavla FOLTYNOVÁ; Tomáš VACULOVIČ; Pavel KRÁSENSKÝ; Viktor KANICKÝ a Radek VYHNÁNEK. \textit{A Multidetection Platform for Proteome Analysis}. Innsbruck, Austria: University of Innsbruck, 2008. 8th Csaba Horváth Medal Award Symposium.

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