コイ肉氷蔵中の筋原繊維タンパク質のATPase活性およびその他の性状変化

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タイトル別名
  • コイ肉氷蔵中の筋原繊維たんぱく質のＡＴＰアーゼ活性およびその他の性状変化
  • Changes in ATPase Activities and Other Properties of Carp Myofibrillar Proteins during Ice-Storage
  • コイ ニク ヒョウゾウチュウ ノ キンゲン センイ タンパクシツ ノ ATPa

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Carp muscle was minced or chopped into small blocks and stored in ice for up to 16 days. Triton-washed myofibrils were prepared from the at-desath and stored muscles.<br> EDTA-ATPase activity of the myofibrils from the minced muscles decreased rapidly, while Ca2+- and Mg2+-ATPase activities decreased gradually during ice-storage with the exception that Mg2+-ATPase activity in the presence of EGTA increased. The increase in this ATPase activity was accompanied with a loss of Ca2+-sensitivity of the myofibrils. Little changes, however, occurred in ATPase activities of the myofibrils from the muscle blocks during ice-storage. SDS-polyacrylamide gel electrophoresis showed that the myofibrils from the fresh and stored muscles were similar in composition.<br> The change in Ca2+-ATPase activity of myosin B obtained from the stored muscles by extraction from the myofibrils paralleled that of the myofibrils during the storage. Mg2+-ATPase activity of the myofibrils from the fresh muscles was higher than that of the myosin B, but this difference reduced with increasing storage period of the muscles. Myosin B. obtained from the stored muscles contained aggregates more than the fresh myosin B. Myosin B aggregates sedimented by centrifugation at 20, 000×g for 20min had higher Mg2+-ATPase activity and lower EDTA-ATPase activity and lower Ca2+-sensitivity than myosin B in supernatant. The viscosity, ATP-sensitivity, and sedimentation behaviour of the myosin B were also measured.

収録刊行物

  • 日本水産学会誌

    日本水産学会誌 46 (2), 207-213, 1980

    公益社団法人 日本水産学会

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