An electrophoretic analysis of protein extracts from normal and dystrophic ovine muscle

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Abstract
A comparison by electrophoretic analysis of extracts from normal and dystrophic ovine muscle has shown qualitative and quantitative differences in the protein composition between normal and affected muscle extracts. There is an enhancement in two components which are thought to be actomyosin and myosin, and a marked decrease in a third component thought to be myogen in extracts from affected longissimus dorsi and quadriceps femoris muscles. These same extracts show an increase in a small, fast-moving component which is probably myoalbumin. Electrophoresis differences were also observed in serum proteins from normal and affected animals. A marked increase in [alpha]-globulin and a decrease in the [beta]-globulin and gamma-globulin fractions were seen. No increase in any serum component could be attributed to the decrease in the muscle-myogen fraction by the criterion of electrophoretic mobility. Similarly, muscle myo-albumin was not found to be the same protein as serum albumin by this criterion.