title: Myosin and actin from ascidian smooth muscle and their interaction.
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.
mesh_terms: D000199:Actins / Q000302:isolation & purification / Q000378:metabolism*; D000205:Actomyosin / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D007700:Kinetics; D009130:Muscle, Smooth / Q000378:metabolism*; D009218:Myosins / Q000302:isolation & purification / Q000378:metabolism*; D011817:Rabbits; D013045:Species Specificity; D014561:Urochordata / Q000378:metabolism*
chemical_list: D000199:Actins; D000205:Actomyosin; D000251:Adenosine Triphosphatases; D009218:Myosins; D000252:Calcium-Transporting ATPases