Studies of a factor from dystrophic mouse muscle inhibitory towards protein synthesis

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Abstract
A substance inhibitory to protein synthesis was purified from mouse skeletal muscle by gel filtration ion-exchange chromatography and centrifugation on sucrose gradients. The MW of the inhibitor, determined by sodium dodecyl sulfate/polyacrylamide-gel electrophoresis, was 71,000. The inhibitory activity was insensitive to RNase A, DNase I and phospholipase C. It was sensitive to pronase treatment but insensitive to heat-treatment and trypsin degradation. The site of action of the inhibitor is probably not on the initiation phase of protein synthesis but rather at a step after the binding of aminoacyl-tRNA to ribosomes. The increased inhibitor activity found in dystrophic muscle is discussed.