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Ultrasonic Enhanced Applications in Proteomics Workflows: single probe versus multiprobe

Author(s): Luz Fernandez | Hugo. M. Santos | J. D. Nunes-Miranda | Carlos Lodeiro | José L. Capelo

Journal: Journal of Integrated OMICS
ISSN 2182-0287

Volume: 1;
Issue: 1;
Start page: 144;
Date: 2011;
Original page

Keywords: Ultrasonic | MALDI | Vitellogenin | Oxygen-18 | Inverse labeling

A 96-well plate-based platform in conjunction with an ultrasonic multiprobe of four tips was assessed to develop various fast proteomics work-flows for gel-based proteomics. The use of such protocols reduce sample time and handling, allowing rapid processing whilst reducing the risk of contamination. The procedure reduces the time to indentify proteins separated by gel electrophoresis to just 8 min/each. In addition, the ultra-sonic multiprobe was compared with the single probe as a tool to obtain high sample throughput in proteomics workflows entailing identifica-tion and/or quantification of proteins using mass-spectrometry based approaches. The 18-O labeling-based method was used to study the type of peptides extracted from the gels when the extraction was done with the aid of ultrasonic energy. The assessment was done in ten standard proteins separated by gel elecrophoresis. Two proteins obtained from D. desulfuricans, and from Cyprinus carpio, Split-Soret cytochrome c, and Vitellogenin respectively, were also indentified as a further proof-of-the concept.
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