Thermal Denaturation of β-Connectin Isolated from Carp Muscle

• Seki Nobuo

  Laboratory of Food Biochemistry, Faculty of Fisheries

• Kumano Yasutaka

  Laboratory of Food Biochemistry, Faculty of Fisheries

書誌事項

タイトル別名

• Thermal Denaturation of β-Connectin Isolated from Carp Muscle
• Thermal Denaturation of ベータ Connectin I

抄録

β-Connectin, a 2, 100 kDa fragment of connectin, was extracted with 0.1M phosphate buffer at pH 6.6 and purified on a Bio-Gel A 50m gel filtration from carp skeletal myofibrils. The isolated connectin was in the native state judging from the fact that it enhanced aggregation of both myosin and actin filaments and appreciably elevated actomyosin Mg-ATPase activity.<br> The thermal denaturation of connectin was measured in 0.1M and 0.6M KCl solutions of neutral pH by means of turbidity. Increase in turbidity was observed at 40°C and occurredmarkedly above 50°C. A physiological concentration of Ca²⁺ and Mg²⁺ did not affect turbidity. Theloss of interaction of connectin with myosin was caused by the denaturation of myosin at lower temperatures rather than that of connectin.

収録刊行物

• Ｆｉｓｈｅｒｉｅｓ　ｓｃｉｅｎｃｅ

  Ｆｉｓｈｅｒｉｅｓ　ｓｃｉｅｎｃｅ 61 (2), 315-319, 1995

  公益社団法人 日本水産学会

キーワード

• muscle protein
• connectin
• titin
• denaturation
• carp

詳細情報

• CRID: 1390001204430213888
• NII論文ID: 130003902677
• NII論文ID: 10004861670
• NII書誌ID: AA10993718
• DOI: 10.2331/fishsci.61.315
• NDL書誌ID: 3641452
• ISSN: 09199268
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I3641452
• Web Site: https://www.jstage.jst.go.jp/article/fishsci1994/61/2/61_2_315/_pdf
• 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