On the cell-free system of protein synthesis from mammalian mitochondria.
Some properties of a submitochondrial cell-free system for protein synthesis are described. The system was prepared from rat liver mitochondria lysed with Triton X-100, and the lysate was characterized by a linear rate of [14C]amino acid incorporation for 15-20 min with subsequent decline in activity. The incorporation reaction was inhibited by chloramphenicol and was insensitive to cycloheximide. Poly(U) addition stimulated [14CA1phenylalanine incorporation by the preincubated submitochondrial system. Upon the addition of 7.5S mRNA that was isolated from mitochondria the major translation product was identified as a hydrophobic poly-peptide which in some properties (solubility in chloroform-methanol mixture) was similar to one of polypeptides synthesized by the sub-mitochondrial system on endogeneous  mRNAs.
D000818:Animals; D002458:Cell Fractionation; D002499:Centrifugation, Density Gradient; D002701:Chloramphenicol / Q000494:pharmacology; D003513:Cycloheximide / Q000494:pharmacology; D003609:Dactinomycin / Q000494:pharmacology; D004996:Ethidium / Q000494:pharmacology; D007700:Kinetics; D008930:Mitochondria, Liver / Q000187:drug effects / Q000378:metabolism*; D010649:Phenylalanine / Q000378:metabolism; D011072:Poly U; D011132:Polyribosomes / Q000378:metabolism; D014176:Protein Biosynthesis; D051381:Rats; D013698:Templates, Genetic
D003609:Dactinomycin; D011072:Poly U; D010649:Phenylalanine; D002701:Chloramphenicol; D003513:Cycloheximide; D004996:Ethidium