Difference between revisions of "Hoejeberg 1977 Biochem Biophys Res Commun"
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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- | |title=Hoejeberg B, Rydstroem J (1977) Purification and molecular properties of reconstitutively active nicotinamide nucleotide transhydrogenase from beef heart mitochondria. Biochem Biophys Res Commun 78:1183-90. | ||
|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 | ||
|organism= | |organism=Bovines | ||
|preparations=Isolated | |tissues=Heart | ||
| | |preparations=Isolated mitochondria | ||
|topics=Inhibitor | |||
|additional=Made history | |additional=Made history | ||
}} | }} | ||
Latest revision as of 12:45, 24 February 2015
| 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
