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J. Biochem, 1984, Vol. 96, No. 4 1027-1031
© 1984 Japanese Biochemical Society

research-article

Superprecipitation of Actomyosin with p-Chloromercuribenzoate-Modified Myosin Reconstituted from Rabbit Skeletal Muscle1

Junji SAGARA2, Yoshiko NISHIMURA, Takenori YAMADA3 and Hiroshi SHIMIZ4

Faculty of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo-ku Tokyo 113

4To whom correspondence should be addressed.

Myosin head modified with p-chloromercuribenzoate (CMB) forms rigor-like complex with actin in the presence of ATP. Actomyosins with CMB-modified myosin were reconstituted to study the effect of rigor-like complexes on superprecipitation. As native myosin was increasingly replaced by CMB-modified myosin, superprecipitation of the actomyosin was strongly suppressed. Further, the suppression of superprecipitation occurred in a different fashion depending on how CMB-modified myosin was incorporated in myosin filaments of the reconstituted actomyosin. The present results indicate that superprecipitation requires the dissociation of actin and myosin head to take place (i.e., the presence of molecular rearrangements of actomyosin network), and further suggest that superprecipitation is associated with dynamic rearrangements of actomyosin network along myosin filaments.

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

2Institute for Chest Disease, Kyoto University, Sakyo-ku, Kyoto, Kyoto 606

3Department of Physiology, School of Medicine, Teikyo University, Itabashi-ku, Tokyo 173


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