Detailed Information on Publication Record
2008
A Multidetection Platform for Proteome Analysis
PREISLER, JanBasic information
Original name
A Multidetection Platform for Proteome Analysis
Name in Czech
A Multidetection Platform for Proteome Analysis
Authors
PREISLER, Jan (203 Czech Republic, guarantor, belonging to the institution)
Edition
Symposium on New Frontiers of Bio-imaging and Micro-separation, Ames, IA, USA, 2008
Other information
Language
English
Type of outcome
Vyžádané přednášky
Field of Study
10406 Analytical chemistry
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
RIV identification code
RIV/00216224:14310/08:00058776
Organization unit
Faculty of Science
Keywords in English
Electrophoresis Capillary; Elemental Analysis; Laser Ablation; Mass Spectrometry; Inductively Coupled Plasma; Speciation
Tags
Tags
International impact
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.
In Czech
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.
Links
| LC06035, research and development project |
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| MSM0021622411, plan (intention) |
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| MSM0021622412, plan (intention) |
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| MSM0021622415, plan (intention) |
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