Stabilization of squid myosin subfragment-1 and myofibrils by ATP-related compounds.

• YOSHIOKA TAKEYA

  Laboratory of Marine Food Science, Graduate School of Fisheries Sciences, Hokkaido University Hokkaido Industrial Technology Center

• KONNO KUNIHIKO

  Laboratory of Marine Food Science, Graduate School of Fisheries Sciences, Hokkaido University

• SEKI NOBUO

  Laboratory of Marine Food Science, Graduate School of Fisheries Sciences, Hokkaido University

抄録

Adenosine triphosphatase (ATPase) inactivation of squid myosin subfragment-1 (S-1) was strongly suppressed upon addition of adenylimidophosphate (AMPPNP), an analogous compound of adenosine triphosphate (ATP); whereas suppression by adenosine diphosphate (ADP) and pyrophosphate (PPi) was not as effective. Adenylimidophosphate did not stabilize myofibrils in which myosin is stabilized by F-actin. Thus, the stabilization effect by F-actin and AMPPNP is not additive. Pyrophosphate markedly accelerated the inactivation of myofibrils through the loss of protection by F-actin. The suppressive effect of F-actin on myosin ATPase inactivation was much greater than that by AMPPNP. The stabilization effects of AMPPNP and F-actin on S-1 were almost completely lost when the medium contained approximately 1 M KCl.

収録刊行物

• Ｆｉｓｈｅｒｉｅｓ　ｓｃｉｅｎｃｅ

  Ｆｉｓｈｅｒｉｅｓ　ｓｃｉｅｎｃｅ 68 (1), 222-226, 2002

  公益社団法人 日本水産学会

キーワード

• adenosine triphosphate
• denaturation
• myofibrils
• myosin
• pyrophosphate
• squid

詳細情報

• CRID: 1390001204428686336
• NII論文ID: 10008272723
• NII書誌ID: AA10993718
• DOI: 10.1046/j.1444-2906.2002.00412.x
• ISSN: 14442906
• ISSN: 09199268
• NDL書誌ID: 6060631
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I6060631
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可