Abstract
Contractile proteins in cat hind limb muscles were studied to examine the possibility that prolonged inactivity of innervated skeletal muscle results in changes in the complement of contractile proteins synthesized by fast- or slow-twich muscles. Myosin light chains and tropomyosins from cat fast- and slow-twitch skeletal muscles were identified in two-dimensional gel electrophoretic patterns. The protein complement synthesized by initially slow-twitch muscle became more similar to that of fast-twitch after long periods (2 to 3 years) of surgically produced inactivity. In some animals slow-twitch forms of myosin light chains and tropomyosins were not seen in normally slow-twitch muscles. These results are in agreement with data obtained in other studies of contractile and biochemical properties of the inactivated muscles.
Published Version
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