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Gonzalez-Halphen, D; Maslov, DA (2004)

NADH-UBIQUINONE OXIDOREDUCTASE ACTIVITY IN THE KINETOPLASTS OF THE PLANT TRYPANOSORNATID PHYTOMONAS SERPENS

PARASITOL RES 92(4):341-346
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NADH-ubiquinone oxidoreductase activity is present in mitochondrial lysates of Phytomonas set-pens. Rotenone at 2-10 muM inhibited the activity 50-75%, indicating that it belongs to respiratory complex I. The activity was also inhibited 50-60% in the presence of 10-30 nM atovaquone suggesting that inhibition of complex I represents a likely mechanism of the known antileishmanial activity of this drug. The complex was partially purified by chromatography on DEAE-Sepharose CL-6B and gel-filtration on Sepharose CL-2B. The NADH:ubiquinone oxidoreductase activity in this preparation was completely inactivated by 20 nM atovaquone. The partially purified complex was present in a low amount and its subunits could not be discerned by staining with Coomassie. However, one of its components, a homologue of the 39 kDa subunit of the bovine complex I, was identified immunochemically in the original lysate and in the partially purified material.