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KMID : 0377519920170020103
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Chung-Ang Journal of Medicine
1992 Volume.17 No. 2 p.103 ~ p.109
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Partial Purification of Myosin from Rabbit Myocardium by Gel Filtration
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Abstract
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Myosin, the major protein required for the production of force and shortening´ in muscle, is a hexamer consisting two heavy chains (molecular mass^-200kDa) and pairs of light chains (molecular mass ^-16 and 20kDa).. Myosin and other contractile apparates from the left ventricular myocardium of rabbit were extracted using pyrophospate buffer system and was ´purified by using the gel filtration. And. partially purified each protein component was confirmed by the electrophoresis in non-dissociating and dissociating conditions respecitively.
On Disc-PAGE of the crude extract, 4 bands clearly appeared and 3 protein components were separated by chromatography in the 5 fractions. In dissociating electrophoresis, each bands were separated into subunit in the pyrophosphate buffer. The first fraction contained the heavy chain of myosin, tropomyosin and myosin light chain 1 and 2.
The second and third fraction were composed of tropomyosin and actin and the proteins that had molecular mass smaller than 15 kDa were in the fourth and fifith fractions.
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