Pyrophosphate-accelerated Actin Denaturation Mechanism in Myofibril

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Actin denaturation upon ATP or pyrophosphate (PPi) addition has been studied in carp myofibril dissolved in 0.5M KCl. ATP-treatment of myofibril remarkably decreased its Mg-ATPase activity with no loss of Ca-ATPase activity. The treated myofibril has a quick inactivation phase in its Ca-ATPase inactivation profile. ATP dissociated myosin from actin. These are all reproduced also by PPi. PPi-induced actin denaturation in the myofibril involves PPi-induced actin dissociation from myosin and a subsequent denaturation of dissociated actin by 0.5 M KCl present in the medium. Ammonium sulfate as high as 1.75M causes no actin denaturation. It was concluded, therefore, that actin is protected from KC1 (or NaCl)-induced denaturation by binding to myosin.

収録刊行物

  • Fisheries science : FS  

    Fisheries science : FS 62(2), 307-311, 1996 

    公益社団法人 日本水産学会

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各種コード

  • NII論文ID(NAID)
    10004865753
  • NII書誌ID(NCID)
    AA10993718
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    09199268
  • NDL 記事登録ID
    3951210
  • NDL 雑誌分類
    ZR26(科学技術--農林水産--水産)
  • NDL 請求記号
    Z54-H592
  • データ提供元
    CJP書誌  CJP引用  NDL  J-STAGE 
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