Binding of cytochrome C to liver mitochondria and microsomes after inhibition of protein biosynthesis with cycloheximide and chloramphenicol.
The inhibition of extramitochondrial biosynthesis with cycloheximide considerably reduces the binding of exogenous cytochrome c to rat liver mitochondria. Tracing the binding of the exogenous cytochrome c to liver mitochondria and microsomal membranes in the period after application of cycloheximide (from 0 to 120 min) shows that the inhibitor evokes inhibition of the binding at the beginning of the period tested and afterwards there is a tendency to reaching the initial level. The above mentioned changes are more pronounced in the case of binding of cytochrome c to mitochondrial membranes. Chloramphenicol does not influence the number of high-affinity cytochrome c binding sites on the mitochondrial membranes. The cytochrome c--mitochondrial membrane complexes become less stable after inhibition of the mitochondrial protein biosynthesis with chloramphenicol.
D000818:Animals; D002701:Chloramphenicol / Q000494:pharmacology*; D003513:Cycloheximide / Q000494:pharmacology*; D003574:Cytochrome c Group / Q000378:metabolism*; D007425:Intracellular Membranes / Q000378:metabolism; D007700:Kinetics; D008297:Male; D008862:Microsomes, Liver / Q000378:metabolism*; D008930:Mitochondria, Liver / Q000378:metabolism*; D014176:Protein Biosynthesis; D051381:Rats
D003574:Cytochrome c Group; D002701:Chloramphenicol; D003513:Cycloheximide