1. 1. Radioactive N,N′-dicyclohexyl carbodiimide (DCCD) is bound as effectively to the N,N′-dicyclohexyl carbodiimide- and oligomycin-sensitive ATPase complex in submitochondrial particles of normal rat liver as to the similar but partially N,N′-dicyclohexyl carbodiimide- and oligomycin-insensitive complex of thiamphenicol-treated rats. The latter complex is deficient in 3 subunits (subunit 6, 7 and 10). 2. 2. Radioactive N,N′-dicyclohexyl carbodiimide is exclusively bound to the subunits present in the bands 8 and 11 of SDS-PAA gels of the purified ATPase complex. These subunits, most likely the dimer and monomer of the N,N′-dicyclohexyl carbodiimide-binding protein, are products of the cytoplasmic protein synthesis. 3. 3. The results together indicate that the N,N′-dicyclohexyl carbodiimide-insensitivity of the ATPase complex formed during in vitro inhibition of mitochondrial protein synthesis, is not caused by a lack of inhibitor binding protein. The same holds for the oligomycin-insensitivity. © 1980.
De Jong, L., Holtrop, M., & Kroon, A. M. (1980). The biogenesis of rat-liver mitochondrial ATPase. Evidence that the N,N′-dicyclohexyl carbodiimide-binding protein is synthesized outside the mitochondria. BBA Section Nucleic Acids And Protein Synthesis, 606(2), 331–337. https://doi.org/10.1016/0005-2787(80)90042-8