Hoejeberg 1977 Biochem Biophys Res Commun
| Hoejeberg B, Rydstroem J (1977) Purification and molecular properties of reconstitutively active nicotinamide nucleotide transhydrogenase from beef heart mitochondria. Biochem Biophys Res Commun 78:1183-90. |
Hoejeberg B, Rydstroem J (1977) Biochem Biophys Res Commun
Abstract: Nicotinamide nucleotide transhydrogenase from beef heart mitochondria was purified to homogeneity and characterized. The enzyme is devoid of other respiratory chain activities as well as flavin. Reduction of NAD+ by NADPH catalyzed by reconstituted transhydrogenase generates an uncoupler-sensitive uptake of lipophilic anions, whereas the rate of reduction of NAD+ by NADPH is enhanced about 13 fold by uncouplers. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate reveales that the protein consists of a single polypeptide of a molecular weight of 97,000. • Keywords: Nicotinamide nucleotide transhydrogenase
Labels:
Organism: Bovines
Tissue;cell: Heart
Preparation: Isolated mitochondria
Regulation: Inhibitor
Made history
