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J. Biochem, 1977, Vol. 81, No. 4 1025-1030
© 1977 Japanese Biochemical Society

research-article

A Study of {gamma} Component, a Myofibrillar Protein

Gaku ASHIBA and Shizuo WATANABE

Department of Chemistry, Faculty of Science, Tokyo Institute of Technology Meguro-ku, Tokyo 152

According to Arai and Watanabe (1968), {gamma} component is a contaminant protein in preparations of skeletal muscle troponin. In the present study we sought to determine whether {gamma} component and creatine kinase [E2.7.3.2.1 are identical. Both {gamma} component and creatine kinase were prepared from chicken breast muscle and compared in four different ways (a, b, c, and d). {gamma} component was shown in each of these ways to be different from creatine kinase.

a) As reported by Lee and Watanabe (1970), {gamma} component was obtained as a DEAE-cellulose flow-through fraction. No creatine kinase activity was detected in this fraction. Using the same conditions as for the {gamma} component preparation, creatine kinase preparations were all retained by DEAE-cellulose. b) In urea-polyacrylamide gel electrophoresis, {gamma} component hardly migrated towards the anode even at pH 9.6, whereas creatine kinase migrated readily. In SDS-polyacrylamide gel electrophoresis both component and creatine kinase migrated similarly, but the migration rate of {gamma} component was slightly faster than that of creatine kinase. c) Ouchterlony's immunodiffusion test with anti-creatine kinase serum of rabbit was performed, and no precipitin line was observed for {gamma} component. d) Component was found to be retained by CM-cellulose, and could thus be purified further by CM-cellulose chromatography with a KCl concentration gradient. The {gamma} component thus purified was used to obtain anti-{gamma} component serum from rabbit, and this antiserum did not form a precipitin line with creatine kinase.


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