Abstract
Cytochrome oxidase was labelled by amino acid incorporation in vivo in the presence and absence of cycloheximide and was isolated by means of Triton X-100, ammonium sulfate fractionation and DEAE-cellulose chromatography from mitochondria of Neurospora crassa. A more than 50-fold purification was achieved with a final gel-filtration step on Bio-Gel. This preparation yielded in disc electrophoresis two distinct bands. In the presence of cycloheximide the purified cytochrome oxidase was not significantly labelled. The conclusion was drawn that the protein moiety of cytochrome oxidase is produced by the cycloheximide sensitive protein synthesizing machinery on the cytoplasmic ribosomes.
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