Abstract
A 72 S ribosome can be isolated from EDTA‐washed mitochondria of Saccharomyces cerevisiae.It easily dissociates into 38 S and 50 S subunits. Incorporation of amino acids into the protein of mitochondria purified in this way is shown to be inhibited by chloramphenicol, while cycloheximide has no effect.When EDTA treatment of the mitochondria is omitted, the mitochondrial fraction contains in addition a special class of 80 S ribosomes, presumably membrane‐bound, which dissociate less easily than the “free” cytoplasmic ribosomes.Incorporation of amino acids into protein of these mitochondria is only partially inhibited by either chloramphenicol or cycloheximide and is stimulated by the addition of a cytoplasmic supernatant.