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J. Biochem, 1988, Vol. 104, No. 5 734-737
© 1988 Japanese Biochemical Society

research-article

Interaction between Chicken Gizzard Caldesmon and Tropomyosin1

Toshihiro Fujii, Jun Ozawa, Yoshiro Ogoma and Yoshiyuki Kondo

Department of Functional Polymer Science, Faculty of Textile Science and Technology, Shinshu University Ueda, Nagano 386

Chicken gizzard muscle caldesmon has been examined for ability to interact with tropomyosin from chicken gizzard muscle by using fluorescence enhancement of tropomyosin labeled with dansyl chloride (DNS) and affinity chromatography. The binding of caldesmon to tropomyosin was regulated by Ca2+ and calmodulin, i.e., at low ionic strength most of the caldesmon bound to tropomyosin-Sepharose 4B was co-eluted by adding calmodulin only in the presence of Ca2+ but not in its absence. This regulation by Ca2+ and calmodulin was also suggested by fluorescence measurements. Actin- and calmodulin-binding sites on the caldesmon molecule were located in the 38K fragment (Fujii, T., Imai, M., Rosenfeld, G.C., & Bryan, J. (1987) J. Blot. Chem. 262,2757–2763). When 38K-enriched fraction was applied to the tropomyosin-Sepharose, the 38K fragment was retained by the column and could be eluted by adding Ca2+ and calmodulin.

1 This work was supported in part by a grant from the Research Foundation for Pharmaceutical Sciences.


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