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Hoejeberg 1977 Biochem Biophys Res Commun

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Publications in the MiPMap
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.

Β» PMID: 921770

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. β€’ Keywords: Nicotinamide nucleotide transhydrogenase


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Organism: Bovines  Tissue;cell: Heart  Preparation: Isolated mitochondria 

Regulation: Inhibitor 



Made history