2008
A Multidetection Platform for Proteome Analysis
PREISLER, JanZákladní údaje
Originální název
A Multidetection Platform for Proteome Analysis
Název česky
A Multidetection Platform for Proteome Analysis
Autoři
PREISLER, Jan (203 Česká republika, garant, domácí)
Vydání
Symposium on New Frontiers of Bio-imaging and Micro-separation, Ames, IA, USA, 2008
Další údaje
Jazyk
angličtina
Typ výsledku
Vyžádané přednášky
Obor
10406 Analytical chemistry
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Kód RIV
RIV/00216224:14310/08:00058776
Organizační jednotka
Přírodovědecká fakulta
Klíčová slova anglicky
Electrophoresis Capillary; Elemental Analysis; Laser Ablation; Mass Spectrometry; Inductively Coupled Plasma; Speciation
Štítky
Příznaky
Mezinárodní význam
Změněno: 11. 4. 2013 09:44, prof. Mgr. Jan Preisler, Ph.D.
V originále
This lecture will describe an instrumentation platform based on a universal interface for deposition of capillary electrophoresis (CE) eluent on a target of a MALDI mass spectrometer. The deposited fractions of proteins or peptides are analyzed off-line 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 enzymatic digestion. Another detection mode is inductively coupled plasma mass spectrometry (ICP MS), which is complementary to soft MALDI MS. We propose substrate-enhanced laser desorption (SELD) for transfer of deposited sample from the target to ICP. Thus, both information about protein identity and content of elements, such as metals or phosphorus is available from a single separation record. Initial results of SELD - ICP OES/MS analysis of metal species will be shown to demonstrate the feasibility of the new approach. Chromium was selected as a model analyte for investigation of the ablation process and demonstration of elemental speciation.
Česky
This lecture will describe an instrumentation platform based on a universal interface for deposition of capillary electrophoresis (CE) eluent on a target of a MALDI mass spectrometer. The deposited fractions of proteins or peptides are analyzed off-line 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 enzymatic digestion. Another detection mode is inductively coupled plasma mass spectrometry (ICP MS), which is complementary to soft MALDI MS. We propose substrate-enhanced laser desorption (SELD) for transfer of deposited sample from the target to ICP. Thus, both information about protein identity and content of elements, such as metals or phosphorus is available from a single separation record. Initial results of SELD - ICP OES/MS analysis of metal species will be shown to demonstrate the feasibility of the new approach. Chromium was selected as a model analyte for investigation of the ablation process and demonstration of elemental speciation.
Návaznosti
| LC06035, projekt VaV |
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| MSM0021622411, záměr |
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| MSM0021622412, záměr |
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| MSM0021622415, záměr |
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