Abstract
The biosynthetic origin of cytochrome oxidase has been studied in yeast using specific inhibitors of mitochondrial and cytoplasmic protein synthesis. Rabbit antiserum against cytochrome oxidase has been employed to selectively precipitate the enzyme from crude Triton extracts of submitochondrial particles. Yeast aerated in derepression medium containing cycloheximide synthesize the three largest subunit proteins of cytochrome oxidase. These proteins are not synthesized when cells are aerated in the presence of chloramphenicol, an inhibitor of mitochondrial protein synthesis. It is concluded that the three largest subunit polypeptides of cytochrome oxidase are translated on mitochondrial ribosomes.
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