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.
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