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  • Title: Myosin and actin from ascidian smooth muscle and their interaction.
    Author: Obinata T, Ooi A, Takano-Ohmuro H.
    Journal: Comp Biochem Physiol B; 1983; 76(3):437-42. PubMed ID: 6227449.
    Abstract:
    Myosin and actin were purified from ascidian smooth muscle. Ascidian myosin contained two classes of light chains and the pH dependence of Ca2+-activated ATPase and the KCl dependence of actin-activated ATPase of ascidian myosin differed from those of vertebrate skeletal myosin. Troponin-tropomyosin complex from ascidian increased the ATPase activity of ascidian reconstituted actomyosin in a Ca2+-dependent manner. Ascidian myosin provided the reconstituted actomyosin with the responsiveness to calcium ions. Two actin isoforms were present in ascidian, which were distinguished by isoelectric points.
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