| Literature DB >> 6227449 |
T Obinata, A Ooi, H Takano-Ohmuro.
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.Entities:
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Year: 1983 PMID： 6227449 DOI： 10.1016/0305-0491(83)90272-9
Source DB: PubMed Journal: Comp Biochem Physiol B ISSN： 0305-0491