title: Cell-free protein synthesis in heart and skeletal muscles from polymyopathic hamsters.
abstract: 1. Cell-free protein synthesis was studied in striated and smooth muscles in an attempt to elucidate the primary genetic defect in polymyopathic hamsters. 2. When washed membrane-free polyribosomes from myopathic and control heart muscle were individually recombined with pH5 enzymes from both types of animals, the pH5 enzymes from myopathic muscle were less active in polypeptide synthesis than those from controls, irrespective of the source of polyribosomes. 3. The same defect was present in skeletal-muscle preparations. 4. Both the initial rate and the maximum extent of incorporation were affected in the defective preparations from myopathic muscle. 5. Concentration differences, with respect to total protein and RNA, were not responsible. 6. Preincubation of the pH5 enzymes resulted in a greater degree of inhibition. 7. The defect in the pH5 enzymes from myopathic muscle was also expressed in poly(U)-directed polyphenylalanine synthesis. 8. Acid proteinase activity in extracts of control and myopathic muscle was the same but general ribonuclease activity in the latter extracts was higher. 9. The defect was also present when both types of pH5 enzymes were prepared in the presence of the ribonuclease-asborbent bentonite. 10. pH5 enzymes from uterine smooth muscle, brains and livers of myopathic animals were similarly affected in homologous and heterologous combinations. 11. It is concluded that the general tissue defect is both qualitative and quantitative in nature, implying that there is a shortage of some essential soluble component in the pH5 fraction which is accompanied by the presence of an altered substituent. This prevents the attainment of extents of polypeptide synthesis in vitro obtained in control extracts from unaffected animals.
mesh_terms: D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000378:metabolism; D002247:Carbon Isotopes; D002474:Cell-Free System; D006224:Cricetinae; D005260:Female; D008099:Liver / Q000378:metabolism; D008297:Male; D009124:Muscle Proteins / Q000096:biosynthesis*; D009130:Muscle, Smooth / Q000378:metabolism; D009132:Muscles / Q000166:cytology / Q000378:metabolism; D009137:Muscular Dystrophy, Animal / Q000378:metabolism*; D009206:Myocardium / Q000166:cytology / Q000378:metabolism*; D009928:Organ Specificity; D010441:Peptide Chain Elongation, Translational; D010442:Peptide Chain Initiation, Translational; D010447:Peptide Hydrolases / Q000378:metabolism; D011132:Polyribosomes / Q000378:metabolism; D012260:Ribonucleases / Q000378:metabolism; D013056:Spectrophotometry, Ultraviolet; D014599:Uterus / Q000378:metabolism
chemical_list: D002247:Carbon Isotopes; D009124:Muscle Proteins; D012260:Ribonucleases; D010447:Peptide Hydrolases; D000604:Amino Acyl-tRNA Synthetases