ABSTRACT
This research is aimed at highlighting the degradation of actin in the Longissimus dorsi muscle of five species, namely, bovine, ovine, caprine, poultry, and freshwater fish. To reveal the degradation of actin, by Western blotting, the myofibrillar proteins of the five studied species were first separated by using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and colored with coomassie brilliant blue G-250. The colored polyacrylamide gel showed a similarity of the bands’ electrophoretic profile in bovine, ovine, and caprine. However, the bands observed in poultry and freshwater fish are specific for each species. The Western blotting revealed the presence of actin fragment of 32 kDa in bovine, ovine, and freshwater fish. A fragment of 28 kDa was found in the five studied species. However, a fragment of 19 kDa was obtained only in caprine. Two fragments of light molecular weights, 15 and 12 kDa, were found in four species such as bovine, ovine, caprine, and poultry. The fragments of 12 and 28 kDa were revealed for the first time by this research, where no previous study has announced their existence.