Abstract
Summary Molybdenum-deficient plants transferred to 185WO4=, incorporate W in protein fractions, normally associated with nitrate reductase (NR.). Plants grown with Mo do not accumulate W in NR. After disc electrophoresis, purified fractions show maximum radioactivity in the expected area of NR. No enzyme was induced by WO4=. NADH-diaphorase was high in Mo deficient and in WO4= treated plants and decreased after induction of NR. by Mo. Inhibition of NR. induction by W results from the formation of a tungstoprotein analogue, lacking NR, activity but active as a diaphorase. Super-induction of NADH-diaphorase by W reflects increased nitrate accumulation. NADH-diaphorase patterns in purified extracts change in distribution and abundance in response to Mo or W treatments.
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