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- W2032026176 abstract "Abstract A molybdenum-containing complex (MCC) has been obtained from NADH-nitrate reductase, partially purified from spinach leaves, by treatment at pH 2.5. The apoprotein of nitrate reductase, which was obtained from leaves of molybdenum-deficient plants grown with nitrate, and ammonium or tungsten or both, retains cytochrome c reductase activity and was shown to react in vitro with MCC to form active nitrate reductase. This was used as a method for estimating the apoprotein content of leaves. Temperature, time and pH conditions for maximum stability of MCC and reconstitution with apoprotein to form active enzyme were determined. Cytochrome c reductases, sedimenting with values of 3.7 S or 8.1 S by sucrose density centrifugation or separated by molecular sieve chromatography, were shown to reconstitute nitrate reductase with MCC. The effect of heat in vivo (> 41 °C) or in vitro (35 °C) was less detrimental to gross cytochrome c reductase activity than to its ability to reconstitute nitrate reductase with MCC. Nitrate reductase adsorbed by AMP-Sepharose was found, using a 185 W analogue marker, to release a low molecular weight metal-containing fraction when washed with phosphate. This fraction appeared to reconstitute nitrate reductase with apoprotein and could be further fractionated into a larger and smaller fragment neither of which could reconstitute the enzyme without the other. The structural and possible significance of these results is discussed." @default.
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- W2032026176 date "1977-08-01" @default.
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- W2032026176 title "Formation of nitrate reductase by recombination of apoprotein fractions from molybdenum-deficient plants with a molybdenum-containing complex" @default.
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