Naslov
Maldi TOF profile of Mytilus galloprovincialis haemolymph proteins

Autori
Perić, Lorena ; Robotti, Elisa ; Boatti, Lara ; Marsano, Francesco ; Negri, Alessandro ; Marengo, Emilio ; Viarengo, Aldo

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Abstracts of the 27th ESCPBnew Congress of the New European Society for Comparative Physiology and Biochemistry "Biological effects of climatic changes and pollution : from biomarkers to system biology" ; u: Comparative biochemistry and physiology. A : molecular & integrative physiology 157 (2010) (S1) S1-S58 ; Session 10: Environmental Proteomics and biomarker discovery S42-S48 ; 15 / - , 2010, S46-S46

Skup
27th ESCPBnew Congress of the New European Society for Comparative Physiology and Biochemistry (27 ; 2010)

Mjesto i datum
Alessandria, Italija, 2010

Vrsta sudjelovanja
Poster

Vrsta recenzije
Nije recenziran

Ključne riječi
Mytilus galloprovincialis ; peptide profiling ; MALDI-TOF

Sažetak
Mussels (Mytilus galloprovincialis) are sentinel species routinely used for monitoring the health status of coastal waters. Mussel’s circulatory fluid (haemolymph) contains secreted proteins as well as proteins coming from the damaged tissue, which could be useful as indicators of risk associated with exposure to environmental contaminants. In this work, we developed a simple procedure for rapid screening of mussel’s haemolymph proteins based on the matrix assisted laser-desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) and chemometric data analysis. To overcome the difficulties related to relatively high dilution of proteins and the presence of salts, an easy and reproducible technique of solid-phase protein extraction was applied, followed by direct elution of sample on the MALDI-target plate. After preliminary optimization of analytical parameters, a sensitive MALDI TOF mass-spectrometry was capable to effectively resolve the low molecular weight haemolymph proteins thanks to their rapid ionization in the < 20 kDa m/z region. Finally, MALDI MS peptide profiling was applied to haemolymph samples of copper - exposed mussels to detect lost and/or gained ions within the MALDI spectra and variations of ions intensity upon treatment. The possibility to use the developed method to monitor the changes in mussel’s haemolymph peptides/proteins profile and to identify new biomarkers related to pathological states of organisms is discussed.

Izvorni jezik
Engleski

Znanstvena područja
Geologija

Napomena
Doi: 10.1016/j.cbpa.2010.06.132

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