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J. Biochem, 1982, Vol. 91, No. 4 1305-1311
© 1982 Japanese Biochemical Society

research-article

Changes in Myosin Isozymes during Development of Chicken Breast Muscle1

Hiromi TAKANO-OHMURO*, Takashi OBINATA*,**, Tomoh MASAKI*,*** and Takashi MIKAWA*,****

*Tokyo Metropolitan Institute of Medical Science Bunkyo-ku, Tokyo 113
**Department of Biology, Faculty of Science, Chiba University Chiba, Chiba 260
***Institute of Basic Medical Sciences, The University of Tsukuba Niihari-gun, Ibaraki 305
****Department of Pharmacology, Faculty of Medicine, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113

The patterns of myosin isozymes in embryonic and adult chicken pectoralis muscle were examined by electrophoresis in a non-denaturing gel system (pyrophosphate acrylamide gel electrophoresis), and both light chains and heavy chains of embryonic and adult myosin isozymes were compared. In pyrophosphate acrylamide gel electrophoresis, the predominant isozyme component in embryonic pectoralis myosin could be clearly distinguished from adult myosin isozymes. SDS-poly-acrylamide gel electrophoresis indicated that the light chain composition of embryonic myosin was also different from that of adult myosin. The pattern of peptide fragments produced by myosin digestion with {alpha}-chymotrypsin differed significantly between embryonic and adult skeletal myosin. These results suggest that myosin in the embryonic pectoralis muscle is different in both light and heavy chain composition from myosin in the same adult tissue.

1This work was supported by a grant from the Ministry of Education, Science and Culture, and by a grant from the National Center for Nervous, Mental and Muscular Disorder (NCNMMD) of the Ministry of Health and Welfare of Japan.


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