Hoejeberg 1977 Biochem Biophys Res Commun: Difference between revisions
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{{Publication | {{Publication | ||
|title=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. | |title=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. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/921770 PMID: 921770] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/921770 PMID: 921770] | ||
|authors=Hoejeberg B, Rydstroem J | |authors=Hoejeberg B, Rydstroem J | ||
|year=1977 | |year=1977 | ||
|journal=Biochem Biophys Res Commun | |journal=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. | |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<sup>+</sup> by NADPH catalyzed by reconstituted transhydrogenase generates an uncoupler-sensitive uptake of lipophilic anions, whereas the rate of reduction of NAD<sup>+</sup> 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= | |keywords=Nicotinamide nucleotide transhydrogenase | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
Revision as of 21:31, 22 June 2012
| 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: Other Mammal"Other Mammal" is not in the list (Human, Pig, Mouse, Rat, Guinea pig, Bovines, Horse, Dog, Rabbit, Cat, ...) of allowed values for the "Mammal and model" property.
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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