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Two-dimensional gel proteome reference map of human small intestine

Maria Paola Simula1 email, Renato Cannizzaro2 email, Maria Dolores Marin1 email, Alessandro Pavan1 email, Giuseppe Toffoli1 email, Vincenzo Canzonieri3 email and Valli De Re1 email

Experimental and Clinical Pharmacology, CRO Centro di Riferimento Oncologico, IRCCS National Cancer Institute, via F. Gallini 2, 33081 Aviano, PN, Italy

Gastroenterology, CRO Centro di Riferimento Oncologico, IRCCS National Cancer Institute, via F. Gallini 2, 33081 AVIANO, PN, Italy

Pathology, CRO Centro di Riferimento Oncologico, IRCCS National Cancer Institute, via F. Gallini 2, 33081 AVIANO, PN, Italy

author email corresponding author email

Proteome Science 2009, 7:10doi:10.1186/1477-5956-7-10

Published: 19 March 2009

Additional files

Additional file 1:

Protein identification results and protein clustering on the basis of their involvement in shared biological pathways. Proteins of human duodenum tissue identified by MALDI-TOF MS from the 2-D gel shown in Figure 1, 2, 3, 4. For every identified protein we reported the Swiss Prot database accession number, protein's molecular weight (MW) and isoelectric point (pI) and the identification results, comprising the number of matching peptides, the extent of sequence coverage and the identification p-value provided by Mascot search engine. We also reported protein spot numbers referring to Figures 1, 2, 3, 4. The list of identified proteins has been analyzed with the Pathway Express tool http://vortex.cs.wayne.edu/projects.htm webcite, or searched against the Entrez Gene database, to find all associated pathways. Proteins have then been grouped on the bases of their involvement in shared biological pathways. Identified proteins resulted involved in metabolic and energetic pathways, in immune response, in the modulation of cell proliferation and apoptosis, in protein's families with structural function and in detoxification reactions.

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Additional file 2:

Duodenal mucosa proteins expression levels. To determine the average expression levels of each identified protein, we extracted, with the XML toolbox of DeCyder software, normalized volumes, for each protein, and for all the five gels tested. Average volume, standard deviation and the coefficient of variation have then been calculated for each protein spot.

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Additional file 3:

Mass spectra raw data and database search results. For spots identifications with a sequence coverage <20% and identification p-values between 0.001 and 0.05, we reported mass spectra raw data and database search results. Mass spectra raw data include centroid mass, peak height, relative peak intensity and peak area. The database search results consist of matching peptides sequences, observed masses and of the mass errors between expected and experimentally observed masses.

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