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J. Biochem, 1976, Vol. 80, No. 2 315-322
© 1976 Japanese Biochemical Society

research-article

{gamma}-Actinin, a New Regulatory Protein from Rabbit Skeletal Muscle I. Purification and Characterization1

Masaaki KURODA and Koscak MARUYAMA

Department of Biophysics, Faculty of Science, Kyoto University Sakyo-ku, Kyoto, Kyoto 606

A new regulatory protein which we have designated as {gamma}-actinin has been isolated from native thin filaments of rabbit skeletal muscle. Depolymerized native thin filaments were fractionated by salting out with ammonium sulfate, and the precipitates obtained at 40–60% ammonium sulfate saturation were further subjected to DEAE-Sephadex and Sephadex G-200 column chromatography. The purified {gamma}-actinin was shown to have a chain weight of 35,000 daltons and had a strong inhibitory action on the polymerization of G-actin. The results of amino acid analysis indicated a unique amino acid composition of {gamma}actinin as compared with other structural proteins of muscle. Non-polar and neutral amino acid residues were abundant. One cysteine residue was contained per one molecule of {gamma}actinin and played a critical role in the maintenance of the inhibitory activity. Pelleting of {gamma}actinin with F-actin showed that {gamma}actinin binds to F-action.

1 This work was supported by grants from the Ministry of Education, Science and Culture, of Japan, and from the Muscular Dystrophy Associations of America, Inc.


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