guanosine-triphosphate and Muscular-Dystrophy--Animal

Topics: Animals; Calcitonin Gene-Related Peptide; Calcium; Cytokines; Cytosol; Glycosylation; GTP-Binding Proteins; Guanosine Triphosphate; Inositol Phosphates; Interferons; Ion Channel Gating; Ion Channels; Muscles; Muscular Dystrophy, Animal; Neurotransmitter Agents; Protein Kinases; Receptors, Nicotinic

Topics: Adenine Nucleotides; Animals; Guanine Nucleotides; Guanosine Diphosphate; Guanosine Triphosphate; Mice; Muscles; Muscular Dystrophy, Animal

Topics: Amino Acids; Animals; Body Weight; Calcium; Cytosol; Guanosine Triphosphate; Heart; Magnesium; Male; Mice; Muscle Proteins; Muscular Dystrophy, Animal; Myocardium; Organ Size; Peptide Elongation Factors; Potassium; Ribosomes; RNA, Transfer; RNA, Transfer, Amino Acyl

The pH 5 supernatant fractions prepared from homogenates of tissues of normal and dystrophic mice were used to study the incorporation of [14C]phenylalanyl-tRNA into peptide. The incorpoation was markedly reduced using the muscle pH 5 supernatant fraction from dystrophic animals but no reduction was seen with brain, liver or heart preparations from dystrophic mice. The lower incorporation with dystrophic muscle pH 5 supernatant was not due to altered activity of ribonuclease, elongation factors, proteolytic enzymes, GTP or sulfhydryl reagents, but was attributable to the presence of activity that was inhibitory to protein synthesis.

Topics: Animals; Brain; Chickens; Dithiothreitol; Guanosine Triphosphate; Kinetics; Liver; Male; Mice; Muscle Proteins; Muscles; Muscular Dystrophy, Animal; Organ Specificity; Peptide Elongation Factors; Protein Biosynthesis; Rats; Ribosomes; Species Specificity