Cytochrome c oxidase is preferentially synthesized in the rough endoplasmic reticulum--mitochondrion complex in rat liver.
The specific activity and content of cytochrome oxidase in the rough endoplasmic reticulum--mitochondrion complex are higher than in the mitochondrial fraction. Radiolabelling studies with the use of hepatocytes and isolated microsomal and rough endoplasmic reticulum--mitochondrion fractions, followed by immunoprecipitation with anti-(cytochrome oxidase) antibody, reveal that the nuclear-coded cytoplasmic subunits of cytochrome oxidase are preferentially synthesized in the latter fraction. The results have a bearing on the mechanism of transport of these subunits into mitochondria.
D000818:Animals; D017936:Cytochrome a Group; D003580:Cytochromes / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000096:biosynthesis*; D004721:Endoplasmic Reticulum / Q000201:enzymology; D066298:In Vitro Techniques; D008099:Liver / Q000166:cytology / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology; D051381:Rats; D013347:Subcellular Fractions / Q000201:enzymology
D017936:Cytochrome a Group; D003580:Cytochromes; D003576:Electron Transport Complex IV