Relevant bibliographies by topics / Aconitate Hydratase

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  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Aconitate Hydratase'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Aconitate Hydratase"

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Hernanz, A., and M. de la Fuente. "Characterization of aconitate hydratase from mitochondria and cytoplasm of ascites tumor cells." Biochemistry and Cell Biology 66, no. 7 (1988): 792–95. http://dx.doi.org/10.1139/o88-090.

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This paper describes the characterization of aconitate hydratase (EC 4.2.1.3) in cytoplasmic and mitochondrial extracts from Ehrlich ascites tumor cells carried by BALB/C mice. The results show a similar distribution of aconitate hydratase in both extracts, with specific activities much lower than those found in pig and mouse tissues. Mitochondrial aconitate hydratase shows a substrate inhibition by citrate with a Km similar to that found in cytoplasm (Km = 1.0 mM and 0.9 mM, respectively). Oxalacetate produces a mixed type of inhibition in both cytoplasmic and mitochondrial aconitate hydratases with different inhibition constants (Ki = 0.3 mM and 1.0 mM, respectively). Moreover, the specific activities of aconitate hydratase in both cytoplasm and mitochondria decrease when the tumor progresses in the peritoneum of BALB/C mice, as well as the percentage of aconitate hydratase activity in the presence of oxalacetate as the inhibitor. These results indicate that the activity and kinetics of aconitate hydratase are markedly altered by neoplastic transformation as occurs in Ehrlich ascites tumor cells. Since aconitate hydratase is not a key enzyme, these unexpected data are of interest in the study of cancer biochemistry.
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Terol, Javier, Guillermo Soler, Manuel Talon, and Manuel Cercos. "The aconitate hydratase family from Citrus." BMC Plant Biology 10, no. 1 (2010): 222. http://dx.doi.org/10.1186/1471-2229-10-222.

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3

Safonova, O. A., T. N. Popova, and L. Saidi. "Citrate influence on oxidative status of rats tissues under experimental toxic hepatitis." Biomeditsinskaya Khimiya 56, no. 4 (2010): 490–98. http://dx.doi.org/10.18097/pbmc20105604490.

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The effect of citrate free-radical oxidation intensity and aconitate hydratase, superoxide dismutase and catalase activities in liver and blood serum of rats with experimental toxic hepatitis has been investigated. Citrate administration to rats with hepatitis decreased biochemiluminescence parameters and conjugated diene content in rats tissues, increased under conditions of CCl4-induced liver damage. At the same time aconitase activity, decreased at the pathology, increases. The superoxide dismutase and catalase activities increased in at experimental toxic hepatitis, tended towards control values after citrate administration.
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Russell, James B., and Neil Forsberg. "Production of tricarballylic acid by rumen microorganisms and its potential toxicity in ruminant tissue metabolism." British Journal of Nutrition 56, no. 1 (1986): 153–62. http://dx.doi.org/10.1079/bjn19860095.

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1. Rumen microorganisms convert trans-aconitate to tricarballylate. The following experiments describe factors affecting the yield of tricarballylate, its absorption from the rumen into blood and its effect on mammalian citric acid cycle activity in vitro.2. When mixed rumen microorganisms were incubated in vitro with Timothy hay (Phleum praiense L.) and 6.7 mM-trans-aconitate, 64 % of the trans-aconitate was converted to tricarballylate. Chloroform and nirate treatments inhibited methane production and increased the yield of tricarballylate to 82 and 75% respectively.3. Sheep given gelatin capsules filled with 20 g trans-aconitate absorbed tricarballylate and the plasma concentration ranged from 0.3 to 0.5 mM 9 h after administration. Feeding an additional 40 g potassium chloride had little effect on plasma tricarballylate concentrations. Between 9 and 36 h there was a nearly linear decline in plasma tricarballylate.4. Tricarballylate was a competitive inhibitor of the enzyme, aconitate hydratase (aconitase; EC 4.2.1.3), and the inhibitor constant, KI, was 0.52 mM. This KIvalue was similar to the Michaelis-Menten constant (Km) of the enzyme for citrate.5. When liver slices from sheep were incubated with increasing concentrations of tricarballylate, [I4C]acetate oxidation decreased. However, even at relatively high concentrations (8 mM), oxidation was still greater than 80% of the maximum. Oxidation of [I4C]acetate by isolated rat liver cells was inhibited to a greater extent by tricarballylate. Concentrations as low as 0.5 mM caused a 30% inhibition of citric acid cycle activity.
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Matasova, L. V., and T. N. Popova. "Aconitate hydratase of mammals under oxidative stress." Biochemistry (Moscow) 73, no. 9 (2008): 957–64. http://dx.doi.org/10.1134/s0006297908090010.

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6

Gorbenko, M. V., T. N. Popova, K. K. Shulgin, S. S. Popov, and A. A. Agarkov. "Effect of melaxen and valdoxan on free radical processes intensity, aconitate hydratase activity and citrate content in rats tissues under hyperthyroidism." Biomeditsinskaya Khimiya 60, no. 4 (2014): 462–68. http://dx.doi.org/10.18097/pbmc20146004462.

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The influence of melaxen and valdoxan on the biochemiluminescence parameters, aconitate hydratase activity and citrate level in rats heart and liver during development of experimental hyperthyroidism has been investigated. Administration of these substances promoted a decrease of biochemiluminescence parameters, which had been increased in tissues of rats in response to the development of oxidative stress under hyperthyroidism. Aconitate hydratase activity and citrate concentration in rats liver and heart, growing at pathological conditions, changed towards control value after administration of the drugs correcting melatonin level. The results indicate the positive effect of valdoxan and melaxen on oxidative status of the organism under the development of experimental hyperthyroidism that is associated with antioxidant action of melatonin.
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7

Popova, T. N., A. A. Agarkov, and A. N. Verevkin. "Intensity of Free Radical Processes in Rat Liver under Type 2 Diabetes and Introduction of Epifamin." Acta Naturae 5, no. 4 (2013): 118–22. http://dx.doi.org/10.32607/20758251-2013-5-4-118-122.

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The effect of epifamin on free radical processes, the activity of caspase-1 and -3, aconitate hydratase and citrate content in rats liver at experimentally induced type 2 diabetes mellitus (T2DM) was studied. The action of epifamin at T2DM leads to a decrease in biochemiluminescence parameters, characterizing the intensity of free radical processes, and changes in aconitase activity and citrate level towards the control. Activities of caspase-1 and caspase-3 in the tissue decreased by a factor of 2.4 and 1.6 in comparison with the levels at the disease. Apparently, epifamin-mediated correction of the level of melatonin, providing a significant antioxidant effect, promotes positive action on the free radical homeostasis.
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8

Brazhnikov, D. A., T. N. Popova, E. D. Kryl`skii, et al. "Effect of 6-hydroxy-2,2,4-trimethyl-1,2-dihydroquinoline on the intensity of free radical processes and the activity of oxidative metabolism enzymes under toxic liver injury in rats." Biomeditsinskaya Khimiya 65, no. 4 (2019): 331–38. http://dx.doi.org/10.18097/pbmc20196504331.

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The effect of 6-hydroxy-2,2,4-trimethyl-1,2-dihydroquinoline on markers of hepatocytes cytolysis (aspartate aminotransferase, alanine aminotransferase and gamma-glutamyl transpeptidase), parameters reflecting the state of oxidative status (intensity of biochemical luminescence and the content of diene conjugates), and the activity of oxidative metabolism enzymes (aconitate hydratase, glucose-6-phosphate dehydrogenase, NADP-isocitrate dehydrogenase) was studied in rats with CCl4-induced liver injury. The results obtained in the course of the work demonstrated the ability of the test compound to reduce the severity of oxidative stress and liver cells damage, as well as to change the activity of aconitate hydratase and NADP-generating enzymes in the direction of control values. 6-hydroxy-2,2,4-trimethyl-1,2-dihydroquinoline was more effective in normalizing CCl4-induced changes of the analyzed parameters that Carsil used as a reference compound. The tendency to normalize the state of oxidative status and enzyme activity of oxidative metabolism can attributed to hepatoprotective and antioxidant properties of the tested compound.
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9

Mead, RJ, MG Feldwick, and JT Bunn. "1,3-Difluoro-2-Propanol: a Potential Replacement for 1080 in Fauna Management Programs in Australia." Wildlife Research 18, no. 1 (1991): 27. http://dx.doi.org/10.1071/wr9910027.

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Administration to rats of 100 mg/kg of 1,3-difluoro-2-propanol (DFP), the major ingredient of the pesticide Gliftor, resulted in citrate accumulation in the kidney after a 3-h lag phase. Inhibition of aconitate hydratase in the kidney and the development of symptoms typical of sodium fluoroacetate (1080) poisoning in DFP-intoxicated rats suggested metabolism of DFP to (-)erythrofluorocitrate. The conversion of DFP to the toxic metabolite was found to involve defluorination by a microsomal mixed-function oxidase in the liver, induced by phenobarbitone and inhibited by piperonyl butoxide. Administration to rats of pyrazole (90 mg/kg body weight) decreased the activity of the mixed-function oxidase-dependent defluorination of DFP. When administered to rats either 2 h before or 2 h after DFP (100 mg/kg body weight) it eliminated symptoms of poisoning, prevented citrate and fluoride accumulation, and decreased aconitate hydratase inhibition in the kidney. The antidotal properties of pyrazole, the mode of toxic action of (-)erythrofluorocitrate, and the potential for DFP to replace 1080 in fauna management programs in Australia is discussed.
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Kiang, Y. T., and C. J. Bult. "Genetic and Linkage Analysis of Aconitate Hydratase Variants in Soybean." Crop Science 31, no. 2 (1991): 322–25. http://dx.doi.org/10.2135/cropsci1991.0011183x003100020020x.

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Dissertations / Theses on the topic "Aconitate Hydratase"

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Brouquisse, Renaud. "Etude des protéines fer-soufre des mitochondries végétales : caractérisation et purification de l'aconitase." Grenoble 1, 1987. http://www.theses.fr/1987GRE10088.

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Les proteines a centre (fe-s) des mitochondries vegetales sont etudiees par resonance para magnetique (rpe), cette etude a permis de caracteriser les centres (fe-s) impliques dans la chaine respiratoire de la membrane interne puis d'etudier et de purifier l'aconitase matricielle. L'activite aconitase dans les cellules d'erable est associee a deux fractions proteique. L'une est presente dans le cytosol alors que la seconde est d'origine mitochondriale. La presence de l'aconitase et de l'isocitrate deshydrogenase nadp-dependante dans le cytosol permet de penser que ces enzymes pourraient avoir un role important dans le metabolisme des acides organiques
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Fan, Rong. "Identification of a sequestered mitochondrial aconitase derived peptide recognized by virus-specific cytolytic T lymphocytes /." 1999. http://wwwlib.umi.com/dissertations/fullcit/9916286.

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Book chapters on the topic "Aconitate Hydratase"

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Schomburg, Dietmar, and Margit Salzmann. "Aconitate hydratase." In Enzyme Handbook 1. Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_131.

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