Abstract
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 dehy drogenase 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...
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Claims 11
Claim · model-written summary
Spinach nitrate reductase and glycolate dehydrogenase activities changed in identical patterns with nitrate availability.
- Taxon
- spinach
Spinacia oleraceae0 - Organ / stage
- leavese0
- Treatment
- nitrate available in the nutrient solutione0
- Gene
- nitrate reductase and glycolate dehydrogenasee0
- Outcome
- Activity of nitrate reductase and glycolate dehydrogenasee0
Not reportedDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“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”
Claim · model-written summary
Replacing nitrate with ammonium caused loss of both enzyme activities in cauliflower.
- Taxon
- cauliflower
Brassica oleracea var. botrytise0 - Treatment
- ammonium ionse0
- Outcome
- activity of both enzymese0
- Direction
- losse0
- Comparator
- nitratee0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Replacing nitrate by ammonium ions caused loss of activity of both enzymes in cauliflower”
Claim · model-written summary
The loss of both enzyme activities after ammonium replacement was less extensive in spinach.
- Taxon
- spinachSpinacia oleraceae0
- Treatment
- ammonium ionse0
- Outcome
- activity of both enzymese0
- Direction
- loss was less extensivee0
- Comparator
- nitratee0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Replacing nitrate by ammonium ions caused loss of activity of both enzymes in cauliflower but this loss was less extensive in spinach plants”
Claim · model-written summary
Both enzyme activities were negligible in molybdenum deficient spinach leaves.
- Taxon
- spinachSpinacia oleraceae0
- Organ / stage
- leavese0
- Treatment
- Mo-deficiente0
- Gene
- Glycolate dehy drogenase and nitrate reductasee0
- Outcome
- Glycolate dehy drogenase and nitrate reductase activitiese0
- Direction
- negligiblee0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Glycolate dehy drogenase and nitrate reductase activities were negligible in Mo-deficient spinach and cauliflower leaves”
Claim · model-written summary
Both enzyme activities were negligible in molybdenum deficient cauliflower leaves.
- Taxon
- cauliflowerBrassica oleracea var. botrytise0
- Organ / stage
- leavese0
- Treatment
- Mo-deficiente0
- Gene
- Glycolate dehy drogenase and nitrate reductasee0
- Outcome
- Glycolate dehy drogenase and nitrate reductase activitiese0
- Direction
- negligiblee0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Glycolate dehy drogenase and nitrate reductase activities were negligible in Mo-deficient spinach and cauliflower leaves”
Claim · model-written summary
Molybdenum addition increased both enzyme activities identically in spinach and cauliflower.
- Taxon
- spinach and cauliflowerSpinacia oleraceaBrassica oleracea var. botrytise0
- Treatment
- addition of Mo to the nutrient mediume0
- Outcome
- Glycolate dehy drogenase and nitrate reductase activitiese0
- Direction
- increasede0
- Comparator
- Mo-deficiente0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Glycolate dehy drogenase 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”
Claim · model-written summary
Tungstate restored both enzyme activities to control levels in molybdenum deficient plants.
Not reportedTaxon
Verbatim
e0“The activity of both enzymes was increased to levels found in control plants when tungstate was added to Mo-deficient plants”
Claim · model-written summary
Phosphate buffer stimulated nitrate reductase activity by 15%.
- Treatment
- Phosphate buffere0
- Gene
- nitrate reductasee0
- Outcome
- nitrate reductasee0
- Direction
- stimulatinge0
- Value
- 15%e0
Not reportedTaxonComparator
Verbatim
e0“Phosphate buffer was found to be the best extraction medium for both enzymes, stimulating nitrate reductase by 15% and glycolate dehydrogenase 3-fold”
Claim · model-written summary
Phosphate buffer stimulated glycolate dehydrogenase activity threefold.
- Treatment
- Phosphate buffere0
- Gene
- glycolate dehydrogenasee0
- Outcome
- glycolate dehydrogenasee0
- Direction
- stimulatinge0
- Value
- 3-folde0
Not reportedTaxonComparator
Verbatim
e0“Phosphate buffer was found to be the best extraction medium for both enzymes, stimulating nitrate reductase by 15% and glycolate dehydrogenase 3-fold”
Claim · model-written summary
The two enzymes had similar pH sensitivity but different thermal denaturation activation energies.
- Outcome
- similar pH sensitivity but differed in their thermal denaturation activation energiese0
Not reportedTaxon
Verbatim
e0“Both enzymes showed a similar pH sensitivity but differed in their thermal denaturation activation energies”
Claim · model-written summary
Gel chromatography indicated a difference in glycolate dehydrogenase protein, but the compared protein is lost to truncation.
Not reportedTaxon
Verbatim
e0“Gel chromatography indicated that glycolate dehydrogenase protein differs from that...”
The same questions in other papers
molybdenum atom · physiology: enzyme activity · Spinacia oleracea (spinach)Results agree
3 papers in the same direction as this paper
- positive
- positive
- positive
Claims are grouped by organism, treatment and what was measured or targeted. A paper counts as positive when any of its claims in the group is positive.