海鞘平滑肌中的肌球蛋白和肌动蛋白及其相互作用。

Myosin and actin from ascidian smooth muscle and their interaction.

作者信息

Obinata T, Ooi A, Takano-Ohmuro H

出版信息

Comp Biochem Physiol B. 1983;76(3):437-42. doi: 10.1016/0305-0491(83)90272-9.

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.

摘要

肌球蛋白和肌动蛋白从海鞘平滑肌中纯化得到。海鞘肌球蛋白含有两类轻链，其Ca2+激活的ATP酶的pH依赖性以及肌动蛋白激活的海鞘肌球蛋白ATP酶的KCl依赖性与脊椎动物骨骼肌肌球蛋白不同。海鞘的肌钙蛋白-原肌球蛋白复合物以Ca2+依赖的方式增加了海鞘重组肌动球蛋白的ATP酶活性。海鞘肌球蛋白使重组肌动球蛋白具有对钙离子的反应性。海鞘中存在两种肌动蛋白异构体，可通过等电点进行区分。