Western blotting is an analytic technique used around the world for many reasons; detecting infections, diseases, and particular proteins in a tissue. When western blotting, first the proteins are extracted and undergo Gel Electrophoresis, next it goes through elecroblotting, and finally detects the proteins. When the results after every step is completed, the membrane is analyzed based on where the bands are present in the gel. It has been told that actin and myosin is present in fish, making it tougher to chew in most cases. To test the theory of actin and myosin being present in fish making it tougher to chew was the purpose of this experiment. The proteins from Rainbow trout, Catfish, Pollock, Salmon, Tilapia, Mahi-mahi, Cod, Lake Erie Perch, KD and Actin/Myosin standard were analyzed in the study and ended up coordinating the findings in the study with the findings in the theory. We discovered that both Actin and Myosin were present in all types of fish and that some fish had more bands than others, thus having more variations. Therefore, proving that our theory was certainly correct about the actin and myosin making the fish tougher to chew. Introduction
The western blot, also known as the protein blot or immunoblot, is a method used to separate proteins by molecular weight. Western blotting is used to detect proteins in a tissue or extract. In a previous experiment a gentleman by the name of K. Nockler and many others were studying an infectious food borne disease called Human Trinchinellosis. Human Trinchinellosis is a disease caused by ingestion of infected pork, meat and other foods in which animals can be exposed to this parasite. He analyzed sera from pigs using a western blot, for the detection of anti-Trichinella-IgG. The results from his experiment using western blotting was that 144 of the sera from pigs were Trichinella-free and 159 pig sera were infected. His study and our experiments are similar, but instead of trying to find a...
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