Isolation and Characterization of Sea Sponge Myosin

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概要

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• Myosin was purified to a homogeneity from sea sponge, Halichondria okadai. The myosin consisted of 220 kDa heavy chain, 18 kDa calcium binding light chain and 21 kDa phosphorylatable light chain. Rotary shadowed images showed the two headed myosin ( myosin II) with a 160 nm tail. The myosin was less soluble in a KCl solution as compared to rabbit skeletal myosin. The K^+ -stimulated and Ca^<2+> -stimulated ATPase activities of sea sponge myosin were 0.46 and 0.07 μmol Pi min^<-1>mg^<-1>, respectively. The Mg^<2+> -activated myosin ATPase activity showed no significant enhancement by the addition of rabbit skeletal muscle actin despite that the light chain was phosphorylated by myosin light chain kinase from chicken gizzard. Sea sponge myosin 18 kDa light chain bound to Ca^<2+> ion but was not phosphorylated like Physarum plasmodia myosin light chains.

• 社団法人日本動物学会の論文
• 1995-12-15

著者

• Kanzawa N

  Department Of Chemistry Faculty Of Science And Technology Sophia University

• Kanzawa Nobuyuki

  Department Of Chemistry Faculty Of Science And Technology Sophia University

• Takano-ohmuro Hiromi

  Department Of Pharmacology Faculty Of Medicine The University Of Tokyo

• Takano-ohmuro Hiromi

  Department Of Pharmacology Faculty Of Medicine University Of Tokyo

• Maruyama Koscak

  Department Of Biology Faculty Of Science Chiba University

• KANZAWA Nobuyuki

  Department of Biology, Faculty of Science, Chiba University

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