Abstract
A nitrate reductase (EC 1.6.6.1)-inactivating factor has been isolated from 8-day-old wheat leaves. The purification schedule involved ammonium sulfate precipitation, Sephadex G-100 filtration, DEAE-cellulose chromatography, and Sephadex G-150 filtration. No accurate assessment could be made as to the degree of purification relative to crude extract as the inactivating factor could not be detected in crude extract. However a 2,446-fold purification was achieved from the ammonium sulfate fraction to the pooled enzyme from the Sephadex G-150 step.The inactivating factor was heat-labile and had a molecular weight of 37,500. The inactivating factor was particularly sensitive to the divalent metal chelators, 1,10-phenanthroline and bathophenanthroline. Evidence indicated that Fe(2+) may be the functional metal. The trypsin inhibitors N-alpha-p-tosyl-l-lysine chloromethyl ketone and alpha-N-benzoyl-l-arginine were inhibitory. However, phenylmethyl sulfonyl fluoride, an inhibitor of serine peptide hydrolases, was not inhibitory. Neither casein nor hemoglobin nor a range of artificial substrates were hydrolyzed by the inactivating factor. Highly purified wheat leaf nitrite reductase (EC 1.7.99.3) and ribulose 1,5-bisphosphate carboxylase:oxygenase (EC 4.1.1.39) were not affected by the nitrate reductase-inactivating factor.The inactivating factor was more active toward the NADH-nitrate reductase compared to either of the component enzymic activities flavin adenine mononucleotide-nitrate reductase and methyl viologen-nitrate reductase. The NADH-ferricyanide reductase (diaphorase) component was the least sensitive.
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Claims 12
Claim · model-written summary
A nitrate reductase inactivating factor was isolated from wheat leaves.
- Taxon
- wheat
Triticum aestivume0 - Organ / stage
- 8-day-old wheat leavese0
- Gene
- nitrate reductase (EC 1.6.6.1)e0
- Outcome
- nitrate reductase (EC 1.6.6.1)-inactivating factore0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“A nitrate reductase (EC 1.6.6.1)-inactivating factor has been isolated from 8-day-old wheat leaves”
Claim · model-written summary
The factor was purified 2,446-fold from the ammonium sulfate fraction.
- Taxon
- WheatTriticum aestivumt0
- Outcome
- purificatione0
- Value
- 2,446-folde0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“a 2,446-fold purification was achieved from the ammonium sulfate fraction to the pooled enzyme from the Sephadex G-150 step”
t0“Wheat Leaves”
Claim · model-written summary
The inactivating factor was heat labile.
- Taxon
- WheatTriticum aestivumt0
- Outcome
- heat-labilee0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The inactivating factor was heat-labile and had a molecular weight of 37,500”
t0“Wheat Leaves”
Claim · model-written summary
The inactivating factor had a molecular weight of 37,500.
- Taxon
- WheatTriticum aestivumt0
- Outcome
- molecular weighte0
- Value
- 37,500e0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The inactivating factor was heat-labile and had a molecular weight of 37,500”
t0“Wheat Leaves”
Claim · model-written summary
Divalent metal chelators inhibited the factor.
- Taxon
- WheatTriticum aestivumt0
- Treatment
- 1,10-phenanthroline and bathophenanthrolinee0
- Outcome
- inactivating factore0
- Direction
- sensitivee0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The inactivating factor was particularly sensitive to the divalent metal chelators, 1,10-phenanthroline and bathophenanthroline”
t0“Wheat Leaves”
Claim · model-written summary
Fe(2+) may be the functional metal.
- Taxon
- WheatTriticum aestivumt0
- Compound
- Fe(2+)e0
- Outcome
- functional metale0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Evidence indicated that Fe(2+) may be the functional metal”
t0“Wheat Leaves”
Claim · model-written summary
Two trypsin inhibitors inhibited the factor.
- Taxon
- WheatTriticum aestivumt0
- Treatment
- N-alpha-p-tosyl-l-lysine chloromethyl ketone and alpha-N-benzoyl-l-argininee0
- Outcome
- inhibitorye0
- Direction
- inhibitorye0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The trypsin inhibitors N-alpha-p-tosyl-l-lysine chloromethyl ketone and alpha-N-benzoyl-l-arginine were inhibitory”
t0“Wheat Leaves”
Claim · model-written summary
Phenylmethyl sulfonyl fluoride was not inhibitory.
- Taxon
- WheatTriticum aestivumt0
- Treatment
- phenylmethyl sulfonyl fluoridee0
- Outcome
- not inhibitorye0
- Direction
- not inhibitorye0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“phenylmethyl sulfonyl fluoride, an inhibitor of serine peptide hydrolases, was not inhibitory”
t0“Wheat Leaves”
Claim · model-written summary
The factor did not hydrolyze the tested protein or artificial substrates.
- Taxon
- WheatTriticum aestivumt0
- Outcome
- casein nor hemoglobin nor a range of artificial substrates were hydrolyzede0
- Direction
- Neithere0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Neither casein nor hemoglobin nor a range of artificial substrates were hydrolyzed by the inactivating factor”
t0“Wheat Leaves”
Claim · model-written summary
Nitrite reductase and RuBisCO were unaffected by the inactivating factor.
- Taxon
- wheatTriticum aestivume0
- Treatment
- nitrate reductase-inactivating factore0
- Outcome
- nitrite reductase (EC 1.7.99.3) and ribulose 1,5-bisphosphate carboxylase:oxygenase (EC 4.1.1.39)e0
- Direction
- not affectede0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Highly purified wheat leaf nitrite reductase (EC 1.7.99.3) and ribulose 1,5-bisphosphate carboxylase:oxygenase (EC 4.1.1.39) were not affected by the nitrate reductase-inactivating factor”
Claim · model-written summary
The factor was more active against NADH nitrate reductase than two component activities.
- Taxon
- WheatTriticum aestivumt0
- Gene
- NADH-nitrate reductasee0
- Outcome
- inactivating factore0
- Direction
- more activee0
- Comparator
- flavin adenine mononucleotide-nitrate reductase and methyl viologen-nitrate reductasee0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The inactivating factor was more active toward the NADH-nitrate reductase compared to either of the component enzymic activities flavin adenine mononucleotide-nitrate reductase and methyl viologen-nitrate reductase”
t0“Wheat Leaves”
Claim · model-written summary
The NADH ferricyanide reductase component was least sensitive.
- Taxon
- WheatTriticum aestivumt0
- Outcome
- NADH-ferricyanide reductase (diaphorase) componente0
- Direction
- least sensitivee0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The NADH-ferricyanide reductase (diaphorase) component was the least sensitive”
t0“Wheat Leaves”
The same questions in other papers
nitrogen · soil: chemistry · Triticum aestivum (wheat)Positive and negative results
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- positive
- positive
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See all 49 papers →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.