Ditgens A, D'Haese J, Small J V, Sobieszek A
J Muscle Res Cell Motil. 1982 Mar;3(1):57-74. doi: 10.1007/BF00711880.
The obliquely striated body wall muscle of the earthworm Lumbricus terrestris L. possesses a dual actin-linked and myosin-linked regulatory system. Tropomyosin from this muscle has now been purified and its functional properties compared to tropomyosin from vertebrate skeletal muscle. Earthworm tropomyosin has a molecular weight of about 70 000 and is composed of two polypeptide chains of molecular weight of 34 000 and 37 000. Structural and functional similarities to skeletal muscle tropomyosin were demonstrated with respect to the formation and periodicity of paracrystals and nets and the potentiation of skeletal muscle acto-SF1 ATPase activity at low ATP concentration. Likewise, earthworm tropomyosin inhibited skeletal muscle acto-HMM ATPase activity at normal ATP concentrations but to a much greater extent than skeletal muscle tropomyosin; this inhibition was removed by skeletal muscle troponin, in the presence of Ca2+. In a system containing earthworm myosin and skeletal muscle actin, earthworm tropomyosin had no detectable influence on the actin-activated ATPase activity. It is concluded that earthworm tropomyosin plays an active role in the actin-linked troponin-dependent regulatory system and has no measurable effect on the regulation via myosin.
蚯蚓(陆正蚓)的斜纹体壁肌肉拥有一个双重的肌动蛋白连接和肌球蛋白连接调节系统。现已纯化了该肌肉的原肌球蛋白,并将其功能特性与脊椎动物骨骼肌的原肌球蛋白进行了比较。蚯蚓原肌球蛋白的分子量约为70000,由两条分子量分别为34000和37000的多肽链组成。在副晶体和网络的形成及周期性以及低ATP浓度下骨骼肌肌动蛋白-SF1 ATP酶活性的增强方面,证明了其与骨骼肌原肌球蛋白在结构和功能上的相似性。同样,蚯蚓原肌球蛋白在正常ATP浓度下抑制骨骼肌肌动蛋白-HMM ATP酶活性,但程度比骨骼肌原肌球蛋白大得多;在Ca2+存在的情况下,骨骼肌肌钙蛋白可消除这种抑制作用。在含有蚯蚓肌球蛋白和骨骼肌肌动蛋白的系统中,蚯蚓原肌球蛋白对肌动蛋白激活的ATP酶活性没有可检测到的影响。得出的结论是,蚯蚓原肌球蛋白在肌动蛋白连接的肌钙蛋白依赖性调节系统中发挥积极作用,而对通过肌球蛋白的调节没有可测量的影响。