Pyrophosphate-accelerated Actin Denaturation Mechanism in Myofibril

• Torigai Makoto

  Laboratory of Food Biochemistry, Faculty of Fisheries, Hokkaido University

• Konno Kunihiko

  Laboratory of Food Biochemistry, Faculty of Fisheries, Hokkaido University

Bibliographic Information

Other Title

• Pyrophosphate accelerated Actin Denatur

Abstract

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.

Journal

• Fisheries science

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

  The Japanese Society of Fisheries Science

Keywords

• actin
• myosin
• myofibril
• ATP
• pyrophosphate
• ammonium sulfate
• denaturation

Details

• CRID: 1390001204427954304
• NII Article ID: 10004865753
• NII Book ID: AA10993718
• DOI: 10.2331/fishsci.62.307
• NDL BIB ID: 3951210
• ISSN: 09199268
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I3951210
• Web Site: https://www.jstage.jst.go.jp/article/fishsci1994/62/2/62_2_307/_pdf
• Text Lang: en
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed