scholarly journals Characteristics of Nicotiana tabacum nitrate reductase protein produced in Saccharomyces cerevisiae

1991 ◽  
Vol 278 (2) ◽  
pp. 393-397 ◽  
Author(s):  
H N Truong ◽  
C Meyer ◽  
F Daniel-Vedele
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nicotiana Tabacum ◽  
Cytochrome C ◽  
Nitrate Reductase ◽  
Higher Plants ◽  
Reductase Activity ◽  
Molybdenum Cofactor ◽  
Biochemical Data ◽  
Native Form ◽  
Nr Activity

Tobacco nitrate reductase (NR) produced in yeast retains cytochrome c reductase activity, but not NR activity. Biochemical data suggest that the haem and FAD domains are functional, and that the molybdenum cofactor (MoCo) domain is inactive owing to the absence of MoCo in yeast. The native form of the produced NR is dimeric. Thus MoCo is not involved in NR dimerization in higher plants, contrary to current assumptions.

scholarly journals Immunochemical characterization of NADPH-cytochrome P-450 reductase from Jerusalem artichoke and other higher plants

1989 ◽  
Vol 259 (3) ◽  
pp. 847-853 ◽  
Author(s):  
I Benveniste ◽  
A Lesot ◽  
M P Hasenfratz ◽  
F Durst
Keyword(s):  
Cytochrome C ◽  
Rat Liver ◽  
Higher Plants ◽  
Polyclonal Antibodies ◽  
Reductase Activity ◽  
Jerusalem Artichoke ◽  
Cross Reactivity ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Cytochrome P 450

Polyclonal antibodies were prepared against NADPH-cytochrome P-450 reductase purified from Jerusalem artichoke. These antibodies inhibited efficiently the NADPH-cytochrome c reductase activity of the purified enzyme, as well as of Jerusalem artichoke microsomes. Likewise, microsomal NADPH-dependent cytochrome P-450 mono-oxygenases (cinnamate and laurate hydroxylases) were efficiently inhibited. The antibodies were only slightly inhibitory toward microsomal NADH-cytochrome c reductase activity, but lowered NADH-dependent cytochrome P-450 mono-oxygenase activities. The Jerusalem artichoke NADPH-cytochrome P-450 reductase is characterized by its high Mr (82,000) as compared with the enzyme from animals (76,000-78,000). Western blot analysis revealed cross-reactivity of the Jerusalem artichoke reductase antibodies with microsomes from plants belonging to different families (monocotyledons and dicotyledons). All of the proteins recognized by the antibodies had an Mr of approx. 82,000. No cross-reaction was observed with microsomes from rat liver or Locusta migratoria midgut. The cross-reactivity generally paralleled well the inhibition of reductase activity: the enzyme from most higher plants tested was inhibited by the antibodies; whereas Gingko biloba, Euglena gracilis, yeast, rat liver and insect midgut activities were insensitive to the antibodies. These results point to structural differences, particularly at the active site, between the reductases from higher plants and the enzymes from phylogenetically distant plants and from animals.

The Determination of Nitrate Reductase Activity of Leaves to the Dominant Species in Forest Community of Northern Aspect of Changbai Mountains

2011 ◽  
Vol 183-185 ◽  
pp. 900-904
Author(s):  
Yu Wen Li ◽  
Yun Jie Wu
Keyword(s):  
Nitrate Reductase ◽  
Tree Species ◽  
Reductase Activity ◽  
Forest Community ◽  
High Yield ◽  
Changbai Mountains ◽  
Ecological Situation ◽  
Nr Activity

This paper addresses the application of improvement in vivo of traditional method for determination of nitrate reductase (NR) activity of leaves to dominant tree species in forest community of northern aspect of Changbai Mountains. It describes the NR activity of tree species related to the shade-endurance and shows that the intolerance tree species has higher NR activity. The NR of a species is also related to the ecological situation of the sites. Tree species with higher NR activities should be selected for breeding of fast growing and high yield tree species.

scholarly journals Structural and functional relationships of enzyme activities induced by nitrate in barley

1970 ◽  
Vol 119 (4) ◽  
pp. 715-725 ◽  
Author(s):  
John L. Wray ◽  
Philip Filner
Keyword(s):  
Cytochrome C ◽  
Nitrate Reductase ◽  
Nitrate Reductase Activity ◽  
Reductase Activity ◽  
Bottom Layer ◽  
Sucrose Density Gradient ◽  
Enzyme Complex ◽  
Cytochrome C Reductase ◽  
Functional Relationships ◽  
Nadh Cytochrome

1. Nitrate induces the development of NADH-nitrate reductase (EC 1.6.6.1), FMNH2–nitrate reductase and NADH–cytochrome c reductase activities in barley shoots. 2. Sucrose-density-gradient analysis shows one band of NADH–nitrate reductase (8S), one band of FMNH2–nitrate reductase activity (8S) and three bands of NADH–cytochrome c reductase activity (bottom layer, 8S and 3.7S). Both 8S and 3.7S NADH–cytochrome c reductase activities are inducible by nitrate, but the induction of the 8S band is much more marked. 3. The 8S NADH–cytochrome c reductase band co-sediments with both NADH–nitrate reductase activity and FMNH2–nitrate reductase activity. Nitrite reductase activity (4.6S) did not coincide with the activity of either the 8S or the 3.7S NADH–cytochrome c reductase. 4. FMNH2–nitrate reductase activity is more stable (t½ 12.5min) than either NADH–nitrate reductase activity (t½ 0.5min) or total NADH–cytochrome c reductase activity (t½ 1.5min) at 45°C. 5. NADH–cytochrome c reductase and NADH–nitrate reductase activities are more sensitive to p-chloromercuribenzoate than is FMNH2–nitrate reductase activity. 6. Tungstate prevents the formation of NADH–nitrate reductase and FMNH2–nitrate reductase activities, but it causes superinduction of NADH–cytochrome c reductase activity. Molybdate overcomes the effects of tungstate. 7. The same three bands (bottom layer, 8S and 3.7S) of NADH–cytochrome c reductase activity are observed irrespective of whether induction is carried out in the presence or absence of tungstate, but only the activities in the 8S and 3.7S bands are increased. 8. The results support the idea that NADH–nitrate reductase, FMNH2–nitrate reductase and NADH–cytochrome c reductase are activities of the same enzyme complex, and that in the presence of tungstate the 8S enzyme complex is formed but is functional only with respect to NADH–cytochrome c reductase activity.

scholarly journals Nitrate Reductase and Soluble Cytochrome c Reductase(s) in Higher Plants

1978 ◽  
Vol 61 (5) ◽  
pp. 748-752 ◽  
Author(s):  
William Wallace ◽  
Christopher B. Johnson
Keyword(s):  
Cytochrome C ◽  
Nitrate Reductase ◽  
Higher Plants ◽  
Cytochrome C Reductase

INFLUENCE DU CLIMAT SUR L’ACTIVITÉ NITRATE RÉDUCTASE AU COURS DU DÉVELOPPEMENT DE SIX VARIÉTÉS D’AVOINE

1989 ◽  
Vol 69 (3) ◽  
pp. 919-923 ◽  
Author(s):  
A. SAUVESTY ◽  
G. GENDRON
Keyword(s):  
Environmental Factors ◽  
Nitrate Reductase ◽  
Plant Development ◽  
Significant Influence ◽  
Environmental Conditions ◽  
Nitrate Reductase Activity ◽  
Nitrate Nitrogen ◽  
Reductase Activity ◽  
Stage Of Development ◽  
Nr Activity

The influence of field climate on nitrate reductase activity (NR) and development was studied in six oat varieties. Of the monitored environmental factors, only temperature had a significant influence; a temperature increase accelerated plant development and increased NR. It was found that a measure of NR activity as early as the coleoptile stage of development indicated optimal environmental conditions for reduction of nitrate nitrogen in a given genotype.Key words: Nitrate reductase activity, development, climate, oat

scholarly journals Effects of growth retarding compounds on chlorophyll accumulation and nitrate reductase activity in nitrate induced cucumber cotyledons

2015 ◽  
Vol 42 (3) ◽  
pp. 431-439 ◽  
Author(s):  
J. S. Knypl
Keyword(s):  
Nitrate Reductase ◽  
Nitrate Reductase Activity ◽  
Reductase Activity ◽  
Chlorophyll Synthesis ◽  
Growth Retardants ◽  
Chlorophyll Accumulation ◽  
High Concentrations ◽  
Amo 1618 ◽  
Nr Activity

Cotyledons were excised from 5-day old etiolated cucumber seedlings and .grown for 24 or 48 h in solutions of plant growth retardants: AMO-1618,B-Nine, CCC and phosfon D, supplemented with KNO<sub>3</sub> (10<sup>-2</sup>M) in light. Nitrate reductase (NR) activity was determined <i>in vivo</i>. CCC and Phosfon D at high concentrations had no effect on nitrate reductase activity in 24 h tests. CCC at 5xl0<sup>-2</sup> M enhanced NR activity in longer 48 h tests; Phosfon D was inhibitory in that case. AMO-1618 markedly decreased NR activity. B-Nine strikingly enhanced NR activity in KNO<sub>3</sub> induced cytoledons; the effect was positively correlated with the concentration of B-Nine. Ali the compounds inhibited chlorophyll synthesis.

scholarly journals THE EFFECT OF PURIFIED AMOUNT OF TRITERPENE GLYCOSIDES AND THEIR ENRICHED EXTRACT FROM LEAVES OF SILPHIUM PERFOLIATUM L. ON THE GROWTH AND ACTIVITY OF NITRATE REDUCTASE OF WIN-TER WHEAT PLANTS

2019 ◽  
pp. 441-448 ◽  
Author(s):  
Eleonora Sergeyevna Davidyants
Keyword(s):  
Nitrate Reductase ◽  
Winter Wheat ◽  
Seed Treatment ◽  
Nitrate Reductase Activity ◽  
Growth Parameters ◽  
Reductase Activity ◽  
Dry Weight ◽  
Potassium Nitrate ◽  
Triterpene Glycosides ◽  
Nr Activity

The effect of seed treatment with solutions of a purified amount of triterpene glycosides (PATG) containing, as major components, oleanolic acid glycosides – sylphiosides B, C, E, G, and extract (E) enriched with sylphiosides, from Silphium perfoliatum L. (Asteraceae) leaves on growth parameters and nitrate reductase activity (NR, EC 1.6.6.1) of 7-day winter wheat plants (Tritium aestivum L.) was studied. It was shown that, seed treatment with PATG solutions in concentrations of 0.0005 and 0.001% and E in concentrations of 0.2 and 0.4% caused an increase in the length of roots, shoots, wet and dry weight of seedlings compared to the control. The stimulating effect of these concentrations of PATG and E on the total nitrate reductase activity of the roots and leaves of seedlings has been established, and an increase in the stimulating effect of preparations on the activity NR оf against the background of substrate activation of the enzyme potassium nitrate (KNO3) was observed. The greatest increase in the total NR activity of roots and leaves of winter wheat plants was observed when PATG acted at a concentration of 0.001% and E – at a concentration of 0.4%, which amounted respectively 122 and 116%, when adding 1 ml of 50 mM KNO3 solution into the growing medium of plants – 141 and 137% relative to the control. The stimulating effect of exogenous triterpene glycosides on NR activity has been established for the first time. The obtained data allow to theoretically substantiate the possibility of practical use of triterpene glycosides and preparations based on them for the regulation of growth and nitrogen metabolism of plants.

In vivo Nitrate Reductase Activity in Leaves of Pearl Millet, Pennisetum americanum (L.) Leeke

1987 ◽  
Vol 14 (2) ◽  
pp. 125 ◽  
Author(s):  
SV Chanda ◽  
AK Joshi ◽  
PN Krishnan ◽  
YD Singh
Keyword(s):  
Nitrate Reductase ◽  
Reductase Activity ◽  
Potassium Phosphate ◽  
Limiting Factor ◽  
Growth Stages ◽  
In Vivo Assay ◽  
Rate Limiting ◽  
Nr Activity

In the in vivo assay of nitrate reductase (NR) in P. americanum leaves, addition of 1% (v/v) Triton X-100, potassium phosphate buffer (80 mM, pH 7.4) and 1.13 mM NADH to the assay medium resulted in maximum activity. With increasing concentration of NADH, saturation-type kinetics were observed. Based on this data metabolic pool concentration for NADH and apparent Km for nitrate reductase were determined. In field studies with cultivars BJ-104, J-104 and 5141-A of P. americanum, the relative limitation of NO3-, NADH and nitrate reductase in NO3- assimilation was determined. NR activity was measured by four modifications of the in vivo assay technique (with NO3-, with NADH, without NO3- and NADH and with both NO3- and NADH additions to the reaction mixture) and with one in vitro technique. For all the cultivars, NADH was the major rate-limiting factor for in vivo assay during early growth stages, while at later stages, NO3- was limiting. At no stage was NR rate-limiting. It is concluded that NR activity alone may not serve as biochemical marker for improved efficiency of utilisation of nitrogen in P. americanum.

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