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J. Biochem, 1992, Vol. 112, No. 6 780-785
© 1992 Japanese Biochemical Society

research-article

Purification and Characterization of Nebulin Subfragments Produced by 0.1 mM CaCl21

Ryuichi Tatsumi, Akihito Hattori and Koui Takahashi

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

Nebulin, which forms a long inextensible filament in sarcomeres, was fragmented into 200-, 160-, 40-, 33-, and 23-kDa subfragments on treatment with 0.1 mM CaCl2. The subfragments released from myofibrils were successfully purified by immunoamnity column chromatography. The 200-, 40-, 33-, and 23-kDa subfragments were released from myofibrils and occupied 80% of the nebulin filaments. The remainder comprised the 180-kDa subfragment bound to the myofibrils. There is a possibility that an entire nebulin filament is constructed from the 200-, 180-, 40-, 33-, and 23-kDa subfragments. We have developed a new "fluorescence-method" to detect the binding of calcium ions to a protein using quin2, and clarified that nebulin is a calcium-binding protein, and that calcium ions bind to the 200-, 40-, and 23-kDa subfragments. Nebulin filaments are probably fragmented on the binding of large amounts of calcium ions to the 200-, 40-, and 23-kDa subfragments.

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


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