A Experiment On Actin And Myosin

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Abstract
Research was conducted on Actin and Myosin protein; chains of amino acid residue responsible for muscle contraction in muscle cells. Through phosphorylation, which causes changes in enzyme activity as result of an alteration in protein conformation, the Myosin Light Chain ½ stimulates and subsequently contracts the smooth muscle. Concentrations of the protein were determined and analyzed among Catfish, Atlantic Salmon, Sockeye Salmon, Shrimp, Red Tuna, Red Snapper, Tilapia, and Wild Cod. Electrophoresis provided a method of visualization of the samples, where Immunodection was then used to identify Actin/Myosin Light Chain ½ proteins. Wild Cod expressed the most Myosin LC ½ protein, whereas Shrimp expressed the least. Furthermore, both Wild Cod and Shrimp differed considerably in comparison to the determined volume intensity of the other seafood samples, which were closer in expression levels with one another. Animal behavior and habitat are factors that have overtime resulted in the overall amount and subsequent use of muscle. Thus analyzing the variance in Actin/Myosin ½ light chain protein expression serves as a tool in understanding adaptation and evolution among species.

Introduction Actin and Myosin proteins serve the primary role of producing muscle contraction. Myosin molecules will create pressure in the skeletal muscle, where ATP hydrolysis causes Myosin to bind to Actin. A conformational change of the molecule then result in Myosin being
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