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J. Biochem, 1989, Vol. 105, No. 6 855-857
© 1989 Japanese Biochemical Society

other

Isolation of Profilin from Embryonic Chicken Skeletal Muscle and Evaluation of Its Interaction with Different Actin Isoforms1

Sumiko Ohshima*, Hiroshi Abe*,** and Takashi Obinata*,2

* Department of Biology, Faculty of Science, Chiba University Chiba, Chiba 260
** Graduate School of Science and Technology, Chiba University Chiba, Chiba 260

2 To whom correspondence should be addressed.

An actin-binding protein of 16 kDa was isolated from embryonic chicken skeletal muscle. The protein had the same properties as profilin, exhibited a much higher affinity for cytoskeletal (ß- and {gamma}-) actins than for sarcomeric ({alpha}-) actin in the embryonic muscle, and inhibited the polymerization of ß- and {gamma}-actins more efficiently in a physiological salt solution. These results indicate that the assembly of cytoskeletal and sarcomeric actins is regulated differently by profilin in the developing skeletal muscle, and that the former may not be involved in myofibril assembly.

1 This work was supported in part by grants from the Shimadzu Science Foundation, the Ministry of Education, Science and Culture, the Ministry of Health and Welfare of Japan, and the Muscular Dystrophy Association of America.


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