A Multidetection Platform for Proteome Analysis

• Authors: PREISLER Jan
• Year of publication: 2008
• MU Faculty or unit: Faculty of Science
• Description: 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.

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