Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.7.1.2 (nitrate reductase)
 3,861 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Nipradilol (NP) was metabolized mainly in liver and denitrated and/or hydroxylated metabolites were formed. NP was not metabolized in heart or lung, and was stable in blood. Denitration of NP was catalysed mainly by glutathione-dependent organic nitrate reductase in liver cytosol, and the hydroxylation was catalysed by liver-microsomal enzymes. Denitration activity for NP was far lower than that for nitroglycerol and isosorbide dinitrate with liver homogenates of several animal species. A marked species difference was found in the denitration activity for NP; dog liver was especially low compared with rabbit, rat and mouse liver.
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PMID:Metabolism of nipradilol by liver homogenates from different species. I. Comparative studies on the denitration of nipradilol and other organic nitrates. 287 57

The nature of the association between nitrate reductase (NR) and membranes was examined. Nitrate reductase activity (NRA) associated with the microsomal fraction of barley (Hordeum vulgare L.) roots amounted to 0.6 to 0.8% of soluble NRA following sonication in the presence of 250 mM KI and repeated osmotic shock. This treatment removed all contaminating soluble NRA from microsomes of uninduced barley roots that had been homogenized in a soluble extract from roots of NO3(-)-induced plants. On continuous sucrose gradients, NRA co-migrated specifically with VO4(-)-sensitive ATPase activity, a plasma membrane (PM) marker; activity of glucose-6-phosphate dehydrogenase, assayed as cytosolic marker, co-migrated with NRA. Microsomal NRA was absent in barley deficient in soluble NR. Perturbation and trypsinolysis experiments with PM vesicles isolated by aqueous two-phase partitioning indicated that NR is associated with the periphery of the cytoplasmic face of the bilayer. These results demonstrate that PM and soluble NRs are essentially the same protein but that the membrane-associated form is tightly bound. Although it is possible that PM-associated NR exists in vivo, unequivocal evidence for this has yet to be shown. However, PM NR is definitely present in vitro.
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PMID:Characterization of the association of nitrate reductase with barley (Hordeum vulgare L.) root membranes. 1153

Latent nitrate reductase activity (NRA) was detected in corn (Zea mays L., Golden Jubilee) root microsome fractions. Microsome-associated NRA was stimulated up to 20-fold by Triton X-100 (octylphenoxy polyethoxyethanol) whereas soluble NRA was only increased up to 1.2-fold. Microsome-associated NRA represented up to 19% of the total root NRA. Analysis of microsomal fractions by aqueous two-phase partitioning showed that the membrane-associated NRA was localized in the second upper phase (U2). Analysis with marker enzymes indicated that the U2 fraction was plasma membrane (PM). The PM-associated NRA was not removed by washing vesicles with up to 1.0 M NACl but was solubilized from the PM with 0.05% Triton X-100. In contrast, vanadate-sensitive ATPase activity was not solubilized from the PM by treatment with 0.1% Triton X-100. The results show that a protein capable of reducing nitrate is embedded in the hydrophobic region of the PM of corn roots.
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PMID:Latent nitrate reductase activity is associated with the plasma membrane of corn roots. 1153 60

Morphological and biochemical interactions between a vesicular-arbuscular mycorrhizal (VAM) fungus (Glomus fasciculatum [Thaxt. sensu Gerdemann] Gerdemann and Trappe) and potato (Solanum tuberosum L.) plants during the development of P deficiency were characterized. Nonmycorrhizal (NM) plants grown for 63 d with low abiotic P supply (0.5 mM) produced 34, 52, and 73% less root, shoot, and tuber dry matter, respectively, than plants grown with high P (2.5 mM). The total leaf area and the leaf area:plant dry weight ratio of low-P plants were substantially lower than those of high-P plants. Moreover, a lower shoot:root dry weight ratio and tuber:plant dry weight ratio in low-P plants than in high-P plants characterized a major effect of P deficiency stress on dry matter partitioning. In addition to a slower rate of growth, low-P plants accumulated nonreducing sugars and nitrate. Furthermore, root respiration and leaf nitrate reductase activity were lower in low-P plants than in high-P plants. Low abiotic P supply also induced physiological changes that contributed to the greater efficiency of P acquisition by low-P plants than by high-P plants. For example, allocation of dry matter and P to root growth was less restricted by P deficiency stress than to shoot and tuber growth. Also, the specific activities of root acid phosphatases and vanadate-sensitive microsomal ATPases were enhanced in P-deficient plants. The establishment of a VAM symbiosis by low-P plants was essential for efficient P acquisition, and a greater root infection level for P-stressed plants indicated increased compatibility to the VAM fungus. By 63 d after planting, low-P VAM plants had recovered 42% more of the available soil P than low-P NM plants. However, the VAM fungus only partially alleviated P deficiency stress and did not completely compensate for inadequate abiotic P supply. Although the specific activities of acid phosphatases and microsomal ATPases were only marginally influenced by VAM infection, VAM roots characteristically had a higher protein concentration and, consequently, enhanced microsomal ATPase and acid phosphatase activities on a fresh weight basis compared with NM roots. Morphological and ultrastructural details of VAM plants are discussed in relation to the influence of the VAM symbiosis on P nutrition of potato.
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PMID:Influence of Vesicular-Arbuscular Mycorrhizal Fungi on the Response of Potato to Phosphorus Deficiency. 1223 74

Isolated cotyledons of fenugreek (Trigonella foenum graecum L.), which respond rapidly and specifically to the application of cytokinins with stimulated expansion, have been used to study the primary action of kinetin. Gross chemical analysis showed that ribonucleic acid increased within 24 hours in response to kinetin application. 8-Azaguanine inhibited both kinetin-induced expansion and RNA synthesis; 5-fluorodeoxyuridine inhibited only the RNA synthesis.Cotyledons produced nitrate reductase activity in response to 20 mm nitrate only in the presence of either light or kinetin and especially in the presence of both. Abscisic acid and inhibitors of RNA and protein synthesis depressed this response. Inhibitors affecting chloroplast development and function did not reduce the response in the presence of light and kinetin.In vitro incorporation of (14)C-l-leucine and (14)C-l-phenyl-alanine into protein by various recombinations of microsomal and 160,000g supernatant fractions varied according to the pretreatment which the cotyledons had received before the preparation of the fractions. Stimulatory effects were mainly associated with the microsomal fractions.The formation of leucine-, valine-, and tyrosine-tRNA complexes by high speed supernatant fractions from differently pretreated cotyledons was also compared. The sharp stimulation of the process by adding tRNA was found to be independent of the kind of preincubation that the cotyledons used for the tRNA extraction had received.It is concluded that the evidence is not in favor of kinetin correcting specific tRNA deficiencies. Kinetin removes a limitation that prevents the synthesis of RNA and genome expression.
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PMID:Action of kinetin on cotyledons of fenugreek. 1665 78

Nitric oxide (NO) is a bioactive molecule involved in many biological events, and has been reported as pro-oxidant as well as anti-oxidant in plants. In the present study, the sources of NO production under water stress, the role of NO in water stress-induced hydrogen peroxide (H2O2) accumulation and subcellular activities of anti-oxidant enzymes in leaves of maize (Zea mays L.) plants were investigated. Water stress induced defense increases in the generation of NO in maize mesphyll cells and the activity of nitric oxide synthase (NOS) in the cytosolic and microsomal fractions of maize leaves. Water stress-induced defense increases in the production of NO were blocked by pretreatments with inhibitors of NOS and nitrate reductase (NR), suggesting that NO is produced from NOS and NR in leaves of maize plants exposed to water stress. Water stress also induced increases in the activities of the chloroplastic and cytosolic anti-oxidant enzymes superoxide dismutase (SOD), ascorbate peroxidase (APX), and glutathione reductase (GR), and the increases in the activities of anti-oxidant enzymes were reduced by pretreatments with inhibitors of NOS and NR. Exogenous NO increases the activities of water stress-induced subcellular anti-oxidant enzymes, which decreases accumulation of H2O2. Our results suggest that NOS and NR are involved in water stress-induced NO production and NOS is the major source of NO. The potential ability of NO to scavenge H2O2 is, at least in part, due to the induction of a subcellular anti-oxidant defense.
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PMID:Nitric oxide reduces hydrogen peroxide accumulation involved in water stress-induced subcellular anti-oxidant defense in maize plants. 1871 46

Latent nitrate reductase activity (NRA) was detected in corn (Zea mays L., Golden Jubilee) root microsome fractions. Microsome-associated NRA was stimulated up to 20-fold by Triton X-100 (octylphenoxy polyethoxyethanol) whereas soluble NRA was only increased up to 1.2-fold. Microsome-associated NRA represented up to 19% of the total root NRA. Analysis of microsomal fractions by aqueous two-phase partitioning showed that the membrane-associated NRA was localized in the second upper phase (U2). Analysis with marker enzymes indicated that the U2 fraction was plasma membrane (PM). The PM-associated NRA was not removed by washing vesicles with up to 1.0 M NACl but was solubilized from the PM with 0.05% Triton X-100. In contrast, vanadate-sensitive ATPase activity was not solubilized from the PM by treatment with 0.1% Triton X-100. The results show that a protein capable of reducing nitrate is embedded in the hydrophobic region of the PM of corn roots.
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PMID:Latent nitrate reductase activity is associated with the plasma membrane of corn roots. 2421 88