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J. Biochem, 1989, Vol. 106, No. 1 110-114
© 1989 Japanese Biochemical Society

research-article

Refined Purification and Characterization of Z-Protein1

Kazuyo Ohashi and Koscak Maruyama

Department of Biology, Faculty of Science, Chiba University Chiba, Chiba 260

Using an improved procedure, Z-protein was prepared from myofibrils of chicken breast muscle. The yield of pure Z-protein increased to 10 mg per kg of muscle. The chain weight of Z-protein was 55, 000 in the presence of SDS. However, Z-protein was eluted before aldolase (Mr 158, 000) in Sephacryl S-400 column chromatography, and, therefore, it appeared to exist as a tetramer in a physiological salt solution. Z-protein had at least four isopeptides whose isoelectric points ranged from pH6.0 to 6.4. Anti-Z-protein antiserum reacted equally with these isopeptides. The extinction coefficient of Z-protein at wavelength 278 nm was 4.2 (1%; light path, lcm). Z-protein which was purified according to this improved method did not bind to F-actin and {alpha}-actinin in a physiological salt solution.

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


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