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Myosin denaturation in heated myofibrils of scallop adductor muscle

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Title: Myosin denaturation in heated myofibrils of scallop adductor muscle
Other Titles: ホタテ閉殻筋筋原線維の加熱によるミオシン変性
Authors: Satoh, Aiko1 Browse this author
Kinoshita, Yasunori2 Browse this author
Konno, Kunihiko3 Browse this author →KAKEN DB
Authors(alt): 佐藤, 亜衣子1
木下, 康宣2
今野, 久仁彦3
Keywords: Scallop
Myosin
Thermal denaturation
Myofibril
Calcium ion
Issue Date: Jan-2013
Publisher: Springer Japan
Journal Title: Fisheries Science
Volume: 79
Issue: 1
Start Page: 149
End Page: 155
Publisher DOI: 10.1007/s12562-012-0565-6
Abstract: Thermal inactivation of Ca2+-ATPase of scallop myofibrils (0.1 M KCl, pH 7.5) was unaffected by the presence of Ca2+. Monomeric myosin and salt-solubility one decreased much faster than Ca2+-ATPase inactivation in both Ca-, and EDTA-media, which was well explained by the faster rod denaturation than subfragment-1 (S-1) denaturation. In contrast, when myofibrils were heated at 0.5 M KCl, slow decrease of salt solubility was characteristic, which was also explained by a slow denaturation of rod portion of myosin. Myofibrils from scallop smooth muscle showed the same denaturation pattern as those from adductor muscle. It was demonstrated that myosin of mollusks is not always stabilized by Ca2+.
ホタテ筋原線維(Mf)のATPase失活は塩濃度上昇で著しく促進されたが、Ca2+添加の影響を受けなかった。この特性はイカMfと異なった。0.1 M KCl中のMf加熱ではATPase失活より速く塩溶解性、単量体ミオシンが減少したが、ミオシンのロッド部位の変性で説明できた。パラミオシンを多量に含むホタテ平滑筋Mfも同じ変性様式を示した。0.5 M KCl中の Mf加熱では塩溶解性は維持され、ロッドの緩やかな変性が対応した。
Rights: © 2013 公益社団法人日本水産学会
The final publication is available at www.springerlink.com
© 2013 The Japanese Society of Fisheries Science
Type: article (author version)
URI: http://hdl.handle.net/2115/51917
Appears in Collections:水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 今野 久仁彦

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