Fragmentation of the denatured carp myosin by calpain and some properties of the fragments.

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  • Muramoto Manabu
    Department of Food Science, Faculty of Fisheries, Hokkaido University
  • Seki Nobuo
    Department of Food Science, Faculty of Fisheries, Hokkaido University

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  • コイ変性ミオシンのカルパイン分解と生成断片の性質
  • コイ ヘンセイ ミオシン ノ カルパイン ブンカイ ト セイセイ ダンペン ノ

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Abstract

When carp myosin was denatured, its heavy chain was cleaved by calpain to give a major fragment of Mr=150, 000 (150k fragment). The same result was obtained from the denatured myosin which had been labeled at SH1 group of the heavy chain with a fluorescent probe 1, 5 IAEDANS. The following results indicated that the 150k fragment corresponds to a major part of the heavy chain of myosin rod segments: (1) the 150k fragment was insoluble at a low ionic strength; (2) it was not released by calpain digestion of heavy meromyosin; (3) it was larger in size than that of the rod prepared by α-chymotryptic digestion; (4) it did not contain the SH1 group.<br>The remainder of the heavy chain including the SH1 group was further digested by calpain to lower molecular weight-fragments.<br>On gel filtration at a high ionic strength where the denatured myosin aggregates and the 150k fragment were fully soluble, it was found that they were eluted together as an indistinguishable single peak, suggesting that they were strongly associated together by non-covalent forces.<br>The significance of the 150k fragment in relation to changes in meat proteins during processing or storage was discussed.

Journal

  • NIPPON SUISAN GAKKAISHI

    NIPPON SUISAN GAKKAISHI 54 (6), 1055-1061, 1988

    The Japanese Society of Fisheries Science

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