A comparison of mitochondrially synthesized proteins from whole mitochondria and cytochrome oxidase in Neurospora.

The four mitochondrial proteins of Neurospora crassa labeled by amino acid incorporation in vivo in the presence of cycloheximide have been characterized with regard to their solubility properties in acidic chloroform-methanol. The labeled proteins are present in pulse-labeled whole mitochondria, pulse-chase labeled whole mitochondria, and a purified preparation of cytochrome oxidase. The labeled proteins in each of these preparations are similar with respect to molecular weight, as determined by dodecylsulfate · polyacrylamide-gel electrophoresis. In addition, proteins of similar molecular weight in each preparation exhibit identical solubility properties in acidic chloroform-methanol. The possibility of the mitochondrially synthesized subunits of cyto-chrome oxidase being representative of total mitochondrial protein synthesis is discussed.

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