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J. Biochem, 1982, Vol. 92, No. 3 809-815
© 1982 Japanese Biochemical Society

research-article

A Myofibrillar Component that Modifies the Actin-Myosin Interaction in Postrigor Skeletal Muscle

Koui TAKAHASHI, Fumio NAKAMURA1 and Mutsuo OKAMOTO

Department of Animal Science, Faculty of Agriculture, Hokkaido University Kita-ku, Sapporo, Hokkaido 060

A protein component that modified the interaction between actin and myosin was released from myofibrils on Ca2+-treatment, accompanying the weakening of Z disks. For its release 10–4 M Ca2+ was required. The presence of the component facilitated the dissociation of thin and thick filaments from myofibrils and delayed superprecipitation of reconstituted actomyosin, independently of Ca2+ concentration. The component is probably a constituent of Z disks. In postmortem muscle, it is possible that the component is released from Z disks with an increased concentration of Ca2+, and that it weakens rigor linkages formed between actin and myosin, giving rise to lengthening of rigor-shortened sarcomeres.

1Present address: Department of Anatomy, Jikei University School of Medicine, Minato-ku, Tokyo 105.


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