Calcium-induced splitting of connectin filaments into β-connectin and a 1,200-kDa subfragment

Koui Takahashi, Akihito Hattori, Ryuichi Tatsumi, Kouji Takai

研究成果: Contribution to journalArticle査読

56 被引用数 (Scopus)


When rabbit skeletal muscle myofibrils were treated with a solution containing 0.1 mM Ca2+ and 30 μg of leupeptin/ml, α-connectin, which forms very thin filaments in myofibrils, was split into β-connectin and a 1,200-kDa subfragment. A part of β-connectin located near the junction between β-connectin and the subfragment seems to have an affinity for calcium ions and to be susceptible to the binding of large amounts of calcium ions. The calcium- binding site on β-connectin is localized near the N2 line in the I band, and the subfragment Is localized adjacent to the Z disk. It is possible that connectin filaments change their elasticity during the contraction-relaxation cycle of skeletal muscle at the physiological concentration of calcium ions. Because postmortem skeletal muscles lose their elasticity and become plastic in association with the calcium-specific splitting of connectin filaments, the splitting is considered to be a factor in meat tenderization during postrigor ageing.

ジャーナルJournal of Biochemistry
出版ステータス出版済み - 1 1 1992

All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学


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