Abstract This experiment used electrophoresis to examine the makeup of muscle proteins from two mammals (cow, Bos taurus; bear, Ursus americanus), two aves (chicken, Gallus gallus; turkey, Meleagris gallopavo), and two fish (King Salmon, Oncorhynchus tshawytscha; Albacore Tuna, Scombridae unclassified).
The hypothesis was that as species have diverged evolutionarily, the makeup of their muscle proteins has also diverged. The further apart two species are evolutionarily, the less their muscle proteins will have in common. The results did not support the hypothesis. There were not enough similarities between the fish proteins and not enough differences between the fish and the shrimp to reach a conclusion as to the commonality of their protein structures.
Introduction
Muscle tissue is composed of as many as 19 different proteins; the largest components are myosin and actin. All muscle tissue contains actin and myosin; these form the fibers that slide past each other as muscles contract and relax. There are also a number of other proteins found in muscle tissue; these other proteins regulate movement, bundle and anchor actin and myosin along with others functions. As species have evolved, they have diverged in the quantities and types of these other proteins (Bio-Rad, 2006). The muscle proteins examined in this experiment were beef (Bos taurus), bear (Ursus americanus), chicken (Gallus gallus), turkey (Meleagris gallopavo), King Salmon (Oncorhynchus tshawytscha), Albacore Tuna (Scombridae unclassified) and shrimp (species unknown); included as an out-group.
The hypothesis of this experiment was that as species diverged evolutionarily, the makeup of their muscle proteins also diverged. The further apart two species are evolutionarily, the less their muscle proteins have in common. If the hypothesis was correct, the two mammalian proteins would be similar, the