Differential expression of sarcoplasmic protein in meat of sheep reared in Continental Southern Italy.

The proteomic analysis defines the identity, the structure and the relative abundance of proteins in a given type of cell and in a spe- cific set of conditions. The analysis of protein profile was carried out to identify possible expression differences of muscular proteins between sheep breeds and use these peculiar profiles as trace back biomarkers. The analyses were carried out on a total of 98 samples of longis- simus dorsi and of leg muscles pools from 49 ovine belonging to five breeds: Altamurana (N=9), Bagnolese (N=10), Gentile di Puglia (N=10), Laticauda (N=10) and Leccese (N=10). The pro- tein profile was investigated using analytical proteomic proce- dures: 2DGE and MALDI-TOF/MS. The two-dimensional maps were compared by image analysis using Image Master 2D-Platinum to define the position and relative intensity (volume %) of every sin- gle spot. In the range of our observation, image analysis highlight- ed 15 spots common to all samples, identified as: Adenilate kinase, DJ-1, Enolase (2 spot), Hemoglobin (Hb), Myoglobin (Myb) (2 spot), Phosphatidilethanolamine binding protein (PEBP), Superoxide dismutase, Triosephosphate isomerase (TPI) (5 spot) and Ubiquitin. With the exception of Enolase, the expression (vol- ume %) of common spots differed between breeds, within the muscle. There were significative (P