1
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Ca2+ activates actin-filament sliding on scallop myosin but inhibits that on Physarum myosin.

      1 , ,
      Journal of biochemistry

      Read this article at

      ScienceOpenPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The actin-activated ATPase activity of Physarum myosin has been shown to be inhibited by microM levels of Ca2+, the mode of which is in contrast to the activating effect of Ca2+ on scallop myosin (Kohama, K. (1987) Adv. Biophys. 23, 149-182 for a review). To determine if Ca2+ regulates ATP-dependent sliding between actin and the myosins, fluorescent actin-filaments were allowed to move on the myosins fixed to a glass surface. The movement on Physarum and scallop myosins was inhibited and activated, respectively, by Ca2+. For this myosin-linked regulation to occur for Physarum myosin, myosin phosphorylation was shown to be a prerequisite.

          Related collections

          Author and article information

          Journal
          J. Biochem.
          Journal of biochemistry
          0021-924X
          0021-924X
          Dec 1989
          : 106
          : 6
          Affiliations
          [1 ] Department of Pharmacology, Faculty of Medicine, University of Tokyo.
          Article
          2534126
          b24600e4-b602-4916-b054-458266312098
          History

          Comments

          Comment on this article