Determination of Primary Structure of Heavy Meromyosin Region of Walleye Pollack Myosin Heavy Chain by cDNA Cloning

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  • Ojima Takao
    Department of Marine Bioresources Chemistry, Faculty of Fisheries, Hokkaido University
  • Kawashima Nagako
    Department of Marine Bioresources Chemistry, Faculty of Fisheries, Hokkaido University
  • Inoue Akira
    Department of Marine Bioresources Chemistry, Faculty of Fisheries, Hokkaido University
  • Amauchi Akiko
    Department of Marine Bioresources Chemistry, Faculty of Fisheries, Hokkaido University
  • Togashi Marie
    Laboratory of Physiological Chemistry and Metabolism, Graduate School of Medicine, The University of Tokyo
  • Watabe Shugo
    Laboratory of Aquatic Molecular Biology and Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo
  • Nishita Kiyoyoshi
    Department of Marine Bioresources Chemistry, Faculty of Fisheries, Hokkaido University

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タイトル別名
  • Determination of Primary Structure of H

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Primary structure of heavy meromyosin region of walleye pollack Theragra chalcogramma myosin heavy chain was determined by cDNA cloning. By using one PCR product and five cDNA clones isolated from a λgt11-cDNA library for the pollack dorsal muscle, a nucleotide sequence of 3, 923 bp comprising 60 bp of 5'-untranslational region and 3, 863 bp of coding region was determined. The deduced sequence of 1, 287 amino acids showed considerably high homology to the corresponding regions of carp myosin (83%) and chicken and rabbit myosins (both 79%). The sequences of the regions for the putative ATP-binding, actin-binding, and regulatory light chain-binding were well conserved among the pollack, carp, chicken, and rabbit myosins (83-100% homology). On the other hand, relatively low sequence homologies were seen in the essential light chain-binding site (52-78%), junctions between 20-kDa and 50-kDa domains (27-33%) and 25-kDa and 50-kDa domains (53-57%) of subfragment-1.

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