Characterization of Myosin Isolated from Bodywall Smooth Muscle of the Annelid, Urechis unicinctus.
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概要
- 論文の詳細を見る
Electron microscopy revealed that bodywall muscle of the annelid Urechis unicinctus consisted of B type smooth muscle cells containing parallel thick (40nm in diameter) and thin (7nm) filaments. Myosin was extracted from Urechis bodywall muscle and purified to homogeneity. Urechis myosin, two-headed myosin, consisted of 200kDa heavy chain and two species of light chains, 24 and 19kDa. The ATPase activity was approximately 0.1μmole/mg/min in the presence of Ca2+ or EDTA. The Mg2+-ATPase activity was remarkably enhanced from 0.005 to 0.2μmole/mg/min by rabbit skeletal muscle actin. EGTA inhibited this actin-activated ATPase activity suggesting that the regulation by calcium ion is of the scallop type.
- 日本学士院の論文
著者
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Matsuno Akira
Department Of Biological Science Faculty Of Life And Environmental Science Shimane University
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Kawamura Yuuki
Department Of Biology Faculty Of Science Chiba University
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Maruyama Koscak
Department Of Biology Faculty Of Science Chiba University
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Matsuno Akira
Department of Biology, Faculty of Science, Shimane University
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KANZAWA Nobuyuki
Department of Biology, Faculty of Science, Chiba University
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