Effects of native thin filaments from sea cucumber on the Mg2+-ATPase activity of myosin

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Abstract

  • 1.

    1. Short native thin filaments were prepared from longitudinal smooth muscle of Stichopus japonicus. During the preparation, appreciable amounts of tropomyosin were dissociated.

  • 2.

    2. The interaction of the short thin filaments with myosin from rabbit skeletal muscle was studied by ATPase measurements.

  • 3.

    3. The Mg2+-ATPase activity of myosin increased with an increase in thin filament concentrations at low molar ratios of actin:myosin (0.25 : 1–4 : 1), whereas the activity decreased to 20–30% of its maximal value at high ratios of actin:myosin (30 : 1–140 : 1).

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Cited by (3)

  • Comparative studies on troponin, a Ca <sup>2+</sup>-dependent regulator of muscle contraction, in striated and smooth muscles of protochordates

    2012, Methods
    Citation Excerpt :

    The resultant precipitate contains actin thin filaments that have tropomyosin and troponin in a considerably high purity (see Fig. 4). By applying slight modification of these procedures, native actin filaments have also been successfully isolated from the muscles of other invertebrate animals such as sea urchin [29], nematodes (Ascaris) [30], sea cucumber [31], earthworm (unpublished data), and tardigrade (water bear) [13]. Troponin and tropomyosin can be dissociated from the isolated actin filaments by incubating the actin filaments in 0.6 M KCl, 1 mM MgCl2 and 10 mM Tris–HCl buffer, pH 7.5 at 4 °C for 1–2 h at 25 °C (Figs. 3 and 5A).

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