Unusual fast myosin isozyme pattern in the lateral gastrocnemius of the chicken

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.