Two calpain inhibiting proteins (calpastatins) in carp skeletal muscle.

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  • YAMADA Yuzo
    Laboratory of Biochemistry, Faculty of Fisheries, Hokkaido University
  • SAKAMOTO Shin-ichi
    Laboratory of Biochemistry, Faculty of Fisheries, Hokkaido University
  • SEKI Nobuo
    Laboratory of Biochemistry, Faculty of Fisheries, Hokkaido University

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Other Title
  • コイ筋肉中の２種類のカルパスタチンの存在とそれらの性質
  • コイ キンニクチュウ ノ 2シュルイ ノ カルパスタチン ノ ソンザイ ト ソ

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Abstract

Calpastatin, a calpain inhibiting protein, was partially purified from carp and rabbit skeletal muscles by essentially the same procedures which consisted of DEAE-cellulose chromatography, heat treatment, CM-cellulose chromatography, and Sephadex G-200 gel filtration, etc.<br>In contrast to rabbit calpastatin which had a molecular weight (MW) of 70, 000 and consisted of two identical subunits; two calpastatins designated H (MW 78, 000) and L (MW 37, 000) were isolated from carp muscle. Each carp calpastatin was a single polypeptide as judged by SDS-polyacrylamide gel electrophoresis and Sephadex G-200 gel filtration. Both carp calpastatins similarly inhibited carp calpains I and II. It was also shown that carp and rabbit calpastatins are acidic-and thermo-stable, and that their inhibitory action against calpain is not associated with sequestering of calcium ions from reaction systems.

Journal

  • NIPPON SUISAN GAKKAISHI

    NIPPON SUISAN GAKKAISHI 51 (6), 1021-1028, 1985

    The Japanese Society of Fisheries Science

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