Using 2‐DE for the differentiation of local chicken breeds

Abstract

The aim of this study was to apply a proteomic approach for the characterisation of local chicken breeds. The experiment involved a total of 29 males of three local Italian chicken breeds: Pépoi, Padovana and Ermellinata di Rovigo. Sarcoplasmic protein fractions of breast muscle were analysed by 2-DE. Image analysis followed by statistical analysis enabled to differentiate groups of individuals based on the similarities of protein expression. Individuals were distinguished into clusters and groups, corresponding to the breed of origin. Distances among individuals, calculated using data on spot volumes, were used to draw a neighbour-joining tree, showing clear individual and breed grouping. The most relevant spots regarding breed differentiation were detected; 11 were identified by MS revealing preliminary evidences on the mechanisms of the breed differentiation process. The results evidenced the ability of proteomic analyses for the characterisation of chicken breeds.

Conservation of Local Turkish and Italian Chicken Breeds: A Case Study

“…For instance, finding pure breeds, funding activities and determining markets for products from these breeds put pressure on the conservation scheme. The strategy to solve these problems must be based on the traceability of animal products and determination of peculiarities of fat composition, and quality of meat and eggs (Zanetti et al, , 2011a(Zanetti et al, , 2011bDe Marchi et al, 2011.…”

Mass spectrometry and animal science: Protein identification strategies and particularities of farm animal species

“…Although it poses relevant issues related to its accuracy, it relies solely on the peptide masses obtained through protease digestion. Mass spectrometers that do not perform fragmentation are cheaper and simple to use, which still makes the PMF identification suitable for a large number of purposes [35,36]. The higher the number of peptides matched with MS or MS/MS data, the higher the statistical confidence obtained for the identification of the selected protein.…”

“…Protein and peptide ions generated by ESI can carry single or multiple charges [36], which are statistically distributed upon their basic sites. This fact is one of the reasons to choose trypsin as a protease for protein digestion prior to identification.…”

“…Although less common in other areas of proteomics, it is still very popular in farm animal muscle research, as witnessed by the number of recent publications that resort to PMF [35,36,103]. In these cases, relatively high success rates were obtained with the PMF identification strategy, as most of the proteins selected for identification were successfully identified.…”

“…In these cases, relatively high success rates were obtained with the PMF identification strategy, as most of the proteins selected for identification were successfully identified. The degree of success of this approach is likely to be directly related to the fact that the species studied: rabbit [103], pig [35] or chicken [36] are either well described or sequenced. Nevertheless, and in the case of rabbit [103] a non-sequenced organism, several proteins were identified in other organisms with special reference to laboratory rats (Rattus norvegicus) and mice (Mus musculus).…”