Abstract
The myosin isozyme composition of the lateral gastrocnemius muscle of the chicken leg was investigated during various stages of development utilizing non-denaturing pyrophosphate gel electrophoresis, two-dimensional gel electrophoresis and peptide mapping techniques. An unusual isoform pattern for fast myosin in the lateral gastrocnemius muscle of the adult chicken leg was demonstrated which consisted of a predominance of myosin homodimers and lesser amounts of myosin heterodimer. In addition, a different myosin heavy chain isoform was present in the adult chicken lateral gastrocnemius muscle when compared to other adult fast-twitch muscles. While the adult lateral gastrocnemius muscle contained a different myosin heavy chain isoform from other adult fast-twitch muscles, the embryonic lateral gastrocnemius muscle contained a myosin heavy chain identical to that of the embryonic pectoralis major.
Published Version
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