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J. Biochem, 1988, Vol. 103, No. 5 809-814
© 1988 Japanese Biochemical Society

research-article

Localization of Paratropomyosin in Skeletal Muscle Myofibrils and Its Translocation during Postmortem Storage of Muscles1

Akihito Hattori, Faculty of Agriculture and Koui Takahashi, Faculty of Agriculture

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

Using polyclonal antibodies against paratropomyosin, which is believed to modify the actin-myosin interaction in postrigor skeletal muscles, we studied the localization of paratropomyosin in chicken breast muscle myofibrils. Intact myofibrils stained with fluorescent antibodies showed that paratropomyosin was exclusively located at the A-I junction region of sarcomeres. In stretched myofibrils (3.7 µm in sarcomere length), the approximate width of the fluorescent stripes and their relation to the A band remained constant. Removal of the A band from myofibrils led to loss of stainability. During postmortem storage of muscles, on the other hand, paratropomyosin was translocated from its original position at the A-I junction region onto thin filaments. The translocation of paratropomyosin was successfully induced with a calcium ion concentration of 10–4 M in the presence of protease inhibitors. We therefore conclude that in postrigor muscles, paratropomyosin is released from the A-I junction region following the increase in the sarcoplasmic calcium ion concentration to 10–4 M, and then binds to thin filaments, which results in weakening of rigor linkages formed between actin and myosin.

1This work was supported in part by a Grant-in-Aid from the Ministry of Education, Science and Culture of Japan.


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