Abstract
The [ 14C]leucine-labeled proteins comprising fast axoplasmic flow of normal and dystrophic mouse sciatic nerve and spinal cord were examined by polyacrylamide-gel electrophoresis. The sciatic nerve showed no qualitative or quantitative differences in protein patterns. The dystrophic sciatic nerve showed increased incorporation of isotope as previously reported (12), and each protein showed increased incorporation of label. The sodium dodecyl sulfate-soluble proteins of the dystrophic spinal cord showed no qualitative but a quantitative change. There was an increase in incorporation of label in the dystrophic compared to the normal spinal cord with the trichoroacetic acid-soluble extract of the dystrophic cord showing a corresponding decrease in specific activity. The possible role of a change of protein turnover in the spinal cord as an influence on the muscle is discussed.
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