A comparative study of nitrate reduction and the oxidation of glycolate

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Abstract

Activity of nitrate reductase and glycolate dehydrogenase in spinach leaves changes in identical patterns following changes in the levels of nitrate available in the nutrient solution of the plants. Replacing nitrate by ammonium ions caused loss of activity of both enzymes in cauliflower but this loss was less extensive in spinach plants. Glycolate dehydrogenase and nitrate reductase activities were negligible in Mo-deficient spinach and cauliflower leaves, but increased to identical extents upon addition of Mo to the nutrient medium. The activity of both enzymes was increased to levels found in control plants when tungstate was added to Mo-deficient plants. Phosphate buffer was found to be the best extraction medium for both enzymes, stimulating nitrate reductase by 15% and glycolate dehydrogenase 3-fold. Both enzymes showed a similar pH sensitivity but differed in their thermal denaturation activation energies. Gel chromatography indicated that glycolate dehydrogenase protein differs from that of nitrate reductase.

Original languageEnglish
Pages (from-to)1-11
Number of pages11
JournalIsrael Journal of Botany
Volume33
Issue number1
DOIs
StatePublished - 1 Jan 1984

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (all)

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