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Sherrard JH, Kennedy JA, Dalling MJ. In Vitro Stability of Nitrate Reductase from Wheat Leaves: III. Isolation and Partial Characterization of a Nitrate Reductase-inactivating Factor. Plant Physiol. 1979;64(4):640-5doi: 10.1104/pp.64.4.640.
Sherrard, J. H., Kennedy, J. A., & Dalling, M. J. (1979). In Vitro Stability of Nitrate Reductase from Wheat Leaves: III. Isolation and Partial Characterization of a Nitrate Reductase-inactivating Factor. Plant physiology, 64(4), 640-5. https://doi.org/10.1104/pp.64.4.640
Sherrard, J H, et al. "In Vitro Stability of Nitrate Reductase from Wheat Leaves: III. Isolation and Partial Characterization of a Nitrate Reductase-inactivating Factor." Plant physiology vol. 64,4 (1979): 640-5. doi: https://doi.org/10.1104/pp.64.4.640
Sherrard JH, Kennedy JA, Dalling MJ. In Vitro Stability of Nitrate Reductase from Wheat Leaves: III. Isolation and Partial Characterization of a Nitrate Reductase-inactivating Factor. Plant Physiol. 1979 Oct;64(4):640-5. doi: 10.1104/pp.64.4.640. PMID: 16661024; PMCID: PMC543152.
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Plant Physiol. 1979 Oct;64(4):640-5. doi: 10.1104/pp.64.4.640.

In Vitro Stability of Nitrate Reductase from Wheat Leaves: III. Isolation and Partial Characterization of a Nitrate Reductase-inactivating Factor.

Plant physiology

J H Sherrard, J A Kennedy, M J Dalling

Affiliations

  1. Plant Sciences Section, School of Agriculture and Forestry, University of Melbourne, Parkville, Victoria, 3052, Australia.

PMID: 16661024 PMCID: PMC543152 DOI: 10.1104/pp.64.4.640

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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