Abstract
Rates of synthesis and turnover of nitrate reductase in Chlorella vulgaris have been estimated from density-labelling experiments. It is demonstrated that nitrate stimulates the rate of turnover of the enzyme. Upon transfer of Chlorella from ammonium to nitrate medium there is a rapid increase in nitrate reductase activity, only part of which is a consequence of increased de novo synthesis: there must also be considerable activation of existing enzyme. It is shown that, in the absence of nitrate, the enzyme is very stable in vivo. Upon transfer from nitrate to ammonium medium, synthesis of nitrate reductase is reduced below the limits of defection. These effects are separate from the reversible (ferricyanide-reactivatable) inactivation of the enzyme which is also observed.
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Abbreviations
- Kat:
-
Katal (One katal is defined as the amount of enzyme which will catalyse the formation of 1 mol of NO-2 s-1 at 25°C)
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Johnson, C.B. Activation, synthesis and turnover of nitrate reductase controlled by nitrate and ammonium in Chlorella vulgaris . Planta 147, 63–68 (1979). https://doi.org/10.1007/BF00384592
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DOI: https://doi.org/10.1007/BF00384592