Rydstroem 1975 Biochem Biophys Res Commun
| Rydstroem J, Kanner N, Racker E (1975) Resolution and reconstitution of mitochondrial nicotinamide nucleotide transhydrogenase. Biochem Biophys Res Commun 67:831-9. |
Rydstroem J, Kanner N, Racker E (1975) Biochem Biophys Res Commun
Abstract: Nicotinamide nucleotide transhydrogenase from bovine heart mitochondria was solubilized with cholate and partially purified by ammoniumsulphate fractionation and density gradient centrifugation. Compared to submitochondrial particles this preparation contained less than 10% of oligomycin-sensitive ATPase and cytochromes. When reconstituted with purified mitochondrial phosphatidylcholine, the enzyme catalyzed a reduction of NAD+ by NADPH that was stimulated by uncouplers and which showed a concomitent uncoupler-sensitive uptake of the lipophilic anion tetraphenylboron, indicating the generation of a membrane potential. It is concluded that transhydrogenase can energize the vesicles directly without the intervention of ATPase or cytochromes. • Keywords: nicotinamide nucleotide transhydrogenase
Labels:
Organism: Bovines
Tissue;cell: Heart
Preparation: Isolated mitochondria
Regulation: ATP
Made history
