コイおよびティラピア背筋ミオシンとウサギ骨格筋ミオシンノlignt Chain

概要

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Comparisons were made by sodium dodecyl sulfate polyacrylamide gel electrophoresis of myosin from dorsal muscle of tilapia, Tilapia mossambica, carp, Cyprinus carpio, and skeletal muscle of rabbit. Consequently significant differences in the molecular weights of the light chains in these myosins were found.Rabbit myosin has three distinct light chains with molecular weights of 25, 000 (LC1), 18, 500 (LC2), and 14, 000 (LC3) respectively. Tilapia myosin contains three light chains, two of which with molecular weight of 25, 000 (LC1) and 14, 000 (LC3) are identical with of rabbit. The other light chain has a molecular weight slightly lower 17, 500 (LC2) than that of rabbit. Carp myosin also has three lingt chains with molecular weights of 25, 000 (LC1), 17, 500(LC2), and 16, 000 (LC3) in which LC3 is clearly different in molecular weightfrom the corresponding light chains of rabbit and tilapia myosins.It was found that, as measured by densitometry, the light chains in myosin from rabbitskeletal, tilapia dorsal, and carp dorsal muscle constituted about 16%, 17%, and 12% of the mass of the myosin molecule, respectively.
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