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

R. Ian Menz | Zendy; David A. Day | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

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

Author(s) -

R. Ian Menz,

David A. Day

Publication year - 1996

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.112.2.607

Subject(s) - dihydrolipoamide dehydrogenase , nad+ kinase , biochemistry , nadh dehydrogenase , dehydrogenase , affinity chromatography , chemistry , polyacrylamide gel electrophoresis , mitochondrion , sodium dodecyl sulfate , ferricyanide , alcohol dehydrogenase , gel electrophoresis , chromatography , enzyme , protein subunit , gene

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research