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PLANT PHYSIOLOGY , Vol 112, Issue 2 607-613, Copyright © 1996 by American Society of Plant Biologists

BIOCHEMISTRY AND ENZYMOLOGY

Identification and Characterization of an Inducible NAD(P)H Dehydrogenase from Red Beetroot Mitochondria

R. I. Menz and D. A. Day
Division of Biochemistry and Molecular Biology and the Cooperative Research Centre for Plant Science, The Australian National University, Canberra, Australian Capital Territory 0200, Australia

Exogenous NADH oxidation of mitochondria isolated from red beetroots (Beta vulgaris L.) increased dramatically upon slicing and aging the tissue. Anion-exchange chromatography of soluble fractions derived by sonication from fresh and aged beetroot mitochondria yielded three NADH dehydrogenase activity peaks. The third peak from aged beetroot mitochondria was separated into two activities by blue-affinity chromatography. One of these (the unbound peak) readily oxidized dihydrolipoamide, whereas the other (the bound peak) did not. The latter was an NAD(P)H dehydrogenase with high quinone and ferricyanide reductase activity and was absent from fresh beet mitochondria. Further affinity chromatography of the NAD(P)H dehydrogenase indicated enrichment of a 58-kD polypeptide on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. We propose that this 58-kD protein is the inducible, external NADH dehydrogenase.


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Copyright © 1996 by the American Society of Plant Biologists