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: 1183-1190. |
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
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Organism: Bovines
Preparation: Isolated Mitochondria"Isolated Mitochondria" is not in the list (Intact organism, Intact organ, Permeabilized cells, Permeabilized tissue, Homogenate, Isolated mitochondria, SMP, Chloroplasts, Enzyme, Oxidase;biochemical oxidation, ...) of allowed values for the "Preparation" property.
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