Relevant bibliographies by topics / Superoxise dismutase

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Superoxise dismutase'

Author: Grafiati
Published: 2 June 2025
Last updated: 31 July 2025

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Journal articles on the topic "Superoxise dismutase"

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Park, Joong-ho, and Jae-heon Kim. "Comparison of enzyme activities of the native and N-terminal 6xHis-tagged Fe supreoxide dismutase from Streptomyces subrutilus P5." Korean Journal of Microbiology 52, no. 2 (2016): 230–35. http://dx.doi.org/10.7845/kjm.2016.6030.

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Öhman, Michael, and Stefan L. Marklund. "Plasma extracellular superoxide dismutase and erythrocyte Cu, Zn-containing superoxide dismutase in alcoholics treated with disulfiram." Clinical Science 70, no. 4 (1986): 365–69. http://dx.doi.org/10.1042/cs0700365.

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1. Disulfiram has long been used in the treatment of chronic alcoholism. It is in vivo partially reduced to diethyldithiocarbamate, which is an efficient inhibitor of Cu, Zn-containing superoxide dismutase both in vitro and in vivo. The recently described extracellular superoxide dismutase is even more sensitive to diethyldithiocarbamate than Cu, Zn-superoxide dismutase. 2. To test for the possibility that long term treatment with disulfiram leads to inhibition of the superoxide dismutases, plasma extracellular superoxide dismutase and erythrocyte Cu, Zn-superoxide dismutase were determined in
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Schäfer, G., and S. Kardinahl. "Iron superoxide dismutases: structure and function of an archaic enzyme." Biochemical Society Transactions 31, no. 6 (2003): 1330–34. http://dx.doi.org/10.1042/bst0311330.

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Iron and manganese superoxide dismutases are phylogenetically closely related. They are compared by in silico analysis with regard to their metal specificity and their three-dimensional structure. Special attention is given to the structure and properties of superoxide dismutases from archaeal prokaryotes. The mechanism and the extreme thermostability of superoxide dismutase from Sulfolobus acidocaldarius are discussed on the basis of its high-resolution X-ray structure. An alternating-site mechanism and an evolutionary origin of superoxide dismutases under the environmental conditions on the
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Gutteridge, J. M. C., and J. V. Bannister. "Copper + zinc and manganese superoxide dismutases inhibit deoxyribose degradation by the superoxide-driven Fenton reaction at two different stages. Implications for the redox states of copper and manganese." Biochemical Journal 234, no. 1 (1986): 225–28. http://dx.doi.org/10.1042/bj2340225.

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When OH. radicals are formed in a superoxide-driven Fenton reaction, in which O2.- is generated enzymically, deoxyribose degradation is effectively inhibited by CuZn- and Mn-superoxide dismutases. The products of this reaction are H2O2 and a Fe3+-EDTA chelate. The mixing of H2O2 and a Fe3+-EDTA chelate also generates OH. radicals able to degrade deoxyribose with the release of thiobarbituric acid-reactive material. This reaction too is inhibited by CuZn- and Mn-superoxide dismutases, suggesting that most of the OH. is formed by a non-enzymic O2.- -dependent reduction of the Fe3+-EDTA chelate.
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Meier, B., C. Michel, M. Saran, J. Hüttermann, F. Parak, and G. Rotilio. "Kinetic and spectroscopic studies on a superoxide dismutase from Propionibacterium shermanii that is active with iron or manganese: pH-dependence." Biochemical Journal 310, no. 3 (1995): 945–50. http://dx.doi.org/10.1042/bj3100945.

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Kinetic studies were performed on the superoxide dismutases isolated from the anaerobic bacterium Propionibacterium shermanii as active enzymes with either iron or manganese, which were naturally incorporated into the same molecule depending on the metal supply. Both the Fe- and Mn- forms showed decreasing activity with increasing pH. This suggests the protonation of some groups near the metal, possibly a metal-bound water molecule. Thus the kinetic behaviour of this superoxide dismutase is much more dependent on the protein structure than on the metal incorporated into the active site. The se
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Hunaiti, A. "Radial Diffusion as a Simple and Rapid Method for Screening Superoxide Dismutase Activity." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 24, no. 5 (1987): 511–12. http://dx.doi.org/10.1177/000456328702400515.

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Superoxide dismutases are of great interest due to their increasing medical applications in therapy and diagnosis of some diseases. The radial diffusion assay was evaluated for its usefulness as a simple, cheap and accurate assay for screening superoxide dismutase activity. In this assay O2− radicals were generated from the interaction of reduced riboflavin with molecular oxygen upon exposure of agar gel containing riboflavin and N,N,N̄,N̄-tetramethylethylene diamine (TEMED) to light. If nitrotctrazolium dye is also present, it will be reduced to the blue insoluble formazan, whilst if superoxi
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BATTISTONI, Andrea, Silvia FOLCARELLI, Roberta GABBIANELLI, Concetta CAPO, and Giuseppe ROTILIO. "The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins." Biochemical Journal 320, no. 3 (1996): 713–16. http://dx.doi.org/10.1042/bj3200713.

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Gel-filtration chromatography experiments performed at high protein concentrations demonstrate that the Cu,Zn superoxide dismutase from Escherichia coli is monomeric irrespective of the buffer and of ionic strength. The catalytic activity of the recombinant enzyme is comparable with that of eukaryotic isoenzymes, indicating that the dimeric structure commonly found in Cu,Zn superoxide dismutases is not necessary to ensure efficient catalysis. The analysis of the amino acid sequences suggests that an altered interaction between subunits occurs in all bacterial Cu,Zn superoxide dismutases. The s
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Canini, Antonella, Patrizia Albertano, Donatella Leonardi, Daniela Di Somma, and Maria Grilli Caiola. "Superoxide dismutase in cyanobacteria of the Baltic Sea." Algological Studies/Archiv für Hydrobiologie, Supplement Volumes 83 (December 19, 1996): 129–43. http://dx.doi.org/10.1127/algol_stud/83/1996/129.

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Battistoni, A. "Role of prokaryotic Cu,Zn superoxide dismutase in pathogenesis." Biochemical Society Transactions 31, no. 6 (2003): 1326–29. http://dx.doi.org/10.1042/bst0311326.

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Several bacterial pathogens possess sodC genes that encode periplasmic or membrane-associated Cu,Zn superoxide dismutases. Since professional phagocytes generate large amounts of reactive oxygen species to control the growth of invading micro-organisms, Cu,Zn superoxide dismutase might protect infectious bacteria from oxy-radical damage and facilitate their survival within the host. This idea has gained support from studies showing that sodC-null mutants of different bacteria are less virulent than their parental wild-type strains, and from the discovery that, despite apparent dispensability f
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Chary, P., D. Dillon, A. L. Schroeder, and D. O. Natvig. "Superoxide dismutase (sod-1) null mutants of Neurospora crassa: oxidative stress sensitivity, spontaneous mutation rate and response to mutagens." Genetics 137, no. 3 (1994): 723–30. http://dx.doi.org/10.1093/genetics/137.3.723.

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Abstract Enzymatic superoxide-dismutase activity is believed to be important in defense against the toxic effects of superoxide. Although superoxide dismutases are among the best studied proteins, numerous questions remain concerning the specific biological roles of the various superoxide-dismutase types. In part, this is because the proposed damaging effects of superoxide are manifold, ranging from inactivation of certain metabolic enzymes to DNA damage. Studies with superoxide-deficient mutants have proven valuable, but surprisingly few such studies have been reported. We have constructed an
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Dissertations / Theses on the topic "Superoxise dismutase"

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Dufernez, Fabienne. "Les superoxyde dismutases des protistes : caractérisation et origine phylogénétique." Lille 2, 2005. http://www.theses.fr/2005LIL2S030.

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Les organismes aérobies ont développé des mécanismes pour se protéger des attaques des espèces activées de l'oxygène produites lors du métabolisme cellulaire. La superoxyde dismutase (SOD) est une métalloenzyme du système de défense anti-oxydant. Elle catalyse la dismutation de l'anion superoxyde en peroxyde d'hydrogène. Les SOD se divisent en 2 grandes familles qui diffèrent fondamentalement d'un point de vue structural : les SOD qui utilisent simultanément le cuivre et le zinc comme métaux cofacteurs (Cu/Zn-SOD) et les SOD utilisant soit le fer (FeSOD) soit le manganèse (MnSOD) comme métal c
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Vinatier, Virginie. "Exploration de la voie péroxynitrite : nouveaux donneurs de NO, étude des superoxyde dimutases à fer et application à la conception d’inhibiteurs." Toulouse 3, 2007. http://www.theses.fr/2007TOU30008.

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Ce travail aborde divers aspects de la chimie du peroxynitrite et de ses précurseurs , le superoxyde et le monoxyde d’azote. Plusieurs donneurs de NO dérivés du SIN-1 ont été synthétisés et étudiés dans le but de diminuer la quantité de péroxynitrite formé pendant la décomposition et d’augmenter la biodisponibilité du NO. Les superoxyde dismutases à fer, enzymes protégeant les protozoaires du stress oxydant, des parasites Plasmodium falciparum, Trypanosoma cruzi et Trypanosoma brucei ont été surexprimées et caractérisées afin de découvrir de nouveaux composés antiparasitaires. La structure de
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Poinso, Alix. "Recherche d'inhibiteurs de la superoxyde dismutase à partir de substances naturelles." Thesis, Toulouse 3, 2016. http://www.theses.fr/2016TOU30378/document.

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Le but de ce travail de thèse était de rechercher de nouvelles molécules inhibitrices de la SOD dans des extraits de substances naturelles. Cette enzyme majeure du stress oxydant étant impliquée dans de nombreux mécanismes de défense des cellules cancéreuses contre l'apoptose représente une voie thérapeutique d'avenir. Nous en avons recherché dans les champignons endophytes de plantes péruviennes, ces micro-organismes produisant de nombreux métabolites de défense des plantes hôtes. Ce travail de thèse a d'abord porté sur l'isolement, la culture, l'identification, l'extraction et la caractérisa
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Olofsson, Eva. "Superoxide dismutase 1 and cataract." Doctoral thesis, Umeå : Umeå universitet, 2009. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-21032.

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Kolahi-Ahari, Ali. "A study of superoxide dismutase activity and superoxide production in kiwifruit." Thesis, University of Canterbury. Biological Sciences, 2006. http://hdl.handle.net/10092/1343.

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The activity of superoxide dismutase (SOD) was determined in three kiwifruit (Actinidia) species including A. deliciosa, A. chinensis, and A. arguta. Among the species tested, the highest SOD activity was found in crude extracts prepared from fruit tissues of A. deliciosa. The highest enzyme activity was localized in seed, followed by locules, core and outer pericarp (OP). SOD activity in crude extract of whole fruit remained stable for at least one month when stored at -20℃. The effect of synthetic protease inhibitors (PI) on SOD activity was investigated. Supplementing crude kiwifruit extrac
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Sinaceur, Jamal Eddine. "Importance des dérivés réduits de l'oxygène dans l'intoxication alcoolique chez le rat : rôle de la desferrioxamine /." Paris : la Documentation française, 1987. http://catalogue.bnf.fr/ark:/12148/cb34926442c.

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Parker, Michael William. "Structural studies on manganese superoxide dismutase." Thesis, University of Oxford, 1985. https://ora.ox.ac.uk/objects/uuid:b8fff51f-1e2f-41b1-baff-4e95b499f0de.

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Superoxide dismutases are widely distributed enzymes which catalyse the dismutation of superoxide radicals to dioxygen and hydrogen peroxide and are considered to be an important agent of an organism's defence against oxygen toxicity. The crystallization and low resolution structure determination of manganese superoxide dismutase (E.G. 1.15.1.1) from Bacillus stearothermophiluB is described. The enzyme crystallized in space group P2<sub>1</sub>2<sub>1</sub>2 with two monomers per asymmetric unit and cell dimensions of ̲a=72.2Å, ̲b=111.1Å and ̲c=51.1Å. The crystals diffracted to beyond 2Ã
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Barkley, Katherine Byer. "Characterization of superoxide dismutase from Actinomyces." Diss., Virginia Polytechnic Institute and State University, 1988. http://hdl.handle.net/10919/53905.

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The anaerobes Actinomyces naeslundii, A. odontolyticus and Actinomyces strain ii E1S.25D produce a Mn-containing superoxide dismutase (MnSOD). Actinomyces, once classified as yeast based on their morphology, are saprophytic organisms found among the normal flora of the mouth but can act as endogenous pathogens resulting in gingivitis and actinomycosis. The ability of Actinomyces to scavenge superoxide may increase survival of the cell from the O₂⁻-dependent killing by polymorphonuclear leukocytes and also enable the organism to be transported through an oxygenated environment from one site to
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Meissner, Felix. "Superoxide dismutase 1 regulates caspase-1." Berlin mbv, 2008. http://d-nb.info/992999286/04.

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Jonsson, P. Andreas. "Superoxide dismutase 1 and amyotrophic lateral sclerosis." Doctoral thesis, Umeå : Medical Biosciences, 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-611.

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Books on the topic "Superoxise dismutase"

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Lester, Packer, ed. Superoxide dismutase. Academic Press, 2002.

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Ingrid, Emerit, Packer Lester, Auclair Christian, and Society for Free Radical Research., eds. Antioxidants in therapy and preventive medicine. Plenum Press, 1990.

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Karlsson, Kurt. Extracellular-superoxide dismutase: Association with glycosaminoglycans. [s.n.], 1988.

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International Conference on Superoxide and Superoxide Dismutase (4th 1985 Rome, Italy). Superoxide and superoxide dismutase in chemistry, biology, and medicine: Proceedings of the 4th International Conference on Superoxide and Superoxide Dismutase, held in Rome, Italy, 1-6 September 1985. Elsevier Science Publishers, 1986.

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Jadot, Guy. Les superoxyde-dismutases: Biochimie, pharmacologie, thérapeutique. Masson, 1988.

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Joyce, Caroline. Superoxide dismutase gene expression in copper deficient rats. The Author], 1992.

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Karpinski, Stanislaw. Copper-zinc superoxide dismutases in Scots pine (Pinus sylvestris L.): Analyses of isoforms, cDNAs and environmental stress responses. Swedish University of Agricultural Sciences, Faculty of Forestry, Dept. of Forest Genetics and Plant Physiology, 1994.

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Murphy, Loretta Mary. XaAFS and EPR studies on Bovine Cu, Zn Superoxide dismutase. University of Manchester, 1995.

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Hough, Michael Alexander. A crystal structure study of CuZn superoxide dismutase from bovine erythrocytes. De Montfort University, 1998.

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Sinaceur, Jamal Eddine. Importance des dérivés réduits de l'oxygène dans l'intoxication alcoolique chez le rat: Rôle de la desferrioxamine. La Documentation française, 1987.

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Book chapters on the topic "Superoxise dismutase"

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Bährle-Rapp, Marina. "Superoxide Dismutase." In Springer Lexikon Kosmetik und Körperpflege. Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71095-0_10232.

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Schomburg, Dietmar, and Dörte Stephan. "Superoxide dismutase." In Enzyme Handbook. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-57942-4_179.

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Gooch, Jan W. "Superoxide Dismutase." In Encyclopedic Dictionary of Polymers. Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_14898.

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Miller, Anne-Frances. "Superoxide Dismutases." In Encyclopedia of Biophysics. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_50.

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Hassan, Hosni Moustafa. "Superoxide Dismutases." In Novartis Foundation Symposia. John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470720622.ch7.

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Cass, A. E. G. "Superoxide Dismutases." In Metalloproteins. Palgrave Macmillan UK, 1985. http://dx.doi.org/10.1007/978-1-349-06372-7_4.

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Fridovich, Irwin. "Superoxide Dismutases." In Advances in Enzymology - and Related Areas of Molecular Biology. John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122860.ch2.

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Fridovich, Irwin. "Superoxide Dismutases." In Advances in Enzymology - and Related Areas of Molecular Biology. John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470123041.ch2.

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Bryngelson, Peter A., and Michael J. Maroney. "Nickel Superoxide Dismutase." In Nickel and Its Surprising Impact in Nature. John Wiley & Sons, Ltd, 2007. http://dx.doi.org/10.1002/9780470028131.ch10.

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Ryan, Kelly C., and Michael J. Maroney. "Nickel Superoxide Dismutase." In Encyclopedia of Metalloproteins. Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_84.

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Conference papers on the topic "Superoxise dismutase"

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Meoni, E., EA Regan, J. Luby, RP Bowler, and JD Crapo. "Extracellular Superoxide Dismutase in COPD and Healthy Smokers." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a4175.

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Ganguly, K., M. Depner, SC Wesselkamper, et al. "Superoxide Dismutase 3, Extracellular (SOD3) Variants and Lung Function." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a1790.

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Ghosh, Sudakshina, Belinda Willard, Suzy A. Comhair, Kulwant S. Aulak, Michael Kinter, and Serpil C. Erzurum. "Janus Function Of Copper-Zinc Superoxide Dismutase In Human Asthma." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a2791.

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Stojiljković, Vesna, Ljubica Gavrilović, Snežana Pejić, et al. "SUPEROXIDE DISMUTASE AND LIPID PEROXIDATION IN CHILDREN AFFECTED BY CELIAC DISEASE." In RAD Conference. RAD Association, 2017. http://dx.doi.org/10.21175/radproc.2017.49.

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Faisal, Muhammad Ali, Salsa Maulida, Siti Intania Mairudi, and Eko Suhartono. "Superoxide dismutase and catalase activity in cataract lens of diabetes mellitus." In INTERNATIONAL CONFERENCE ON BIOINFORMATICS AND NANO-MEDICINE FROM NATURAL RESOURCES FOR BIOMEDICAL RESEARCH: 3rd Annual Scientific Meeting for Biomedical Sciences. AIP Publishing, 2019. http://dx.doi.org/10.1063/1.5110016.

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Schwindt, CD, S. Leu, F. Zaldivar, and DM Cooper. "Brief Exercise Decreases Superoxide Dismutase in Healthy, but Not Asthmatic Children." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a1289.

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Cui, Ye, Jennifer Robertson, Shyam Maharaj, et al. "Gene Transfer Of Extracellular Superoxide Dismutase Ameliorates Pulmonary Fibrosis In Rats." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2003.

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Xiaoming Hang, Cong Liu, Yang Liu, and Yeqing Sun. "Joint toxic effects of naphthalene and cadmium on zebrafish superoxide dismutase." In 2011 International Conference on Remote Sensing, Environment and Transportation Engineering (RSETE). IEEE, 2011. http://dx.doi.org/10.1109/rsete.2011.5964306.

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Ghosh, Sudakshina, Belinda Willard, Suzy Comhair, et al. "Redox Dependent Function Of Copper-Zinc Superoxide Dismutase In Human Asthma." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a4960.

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Mizushima, Tohru, and Ken-ichiro Tanaka. "Protective And Therapeutic Effects Of Lecithinized Superoxide Dismutase Against Pulmonary Fibrosis." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a5180.

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Reports on the topic "Superoxise dismutase"

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Champaigne, Rachel. The Role of Mitochondrial Superoxide Dismutase (SOD2) During a Coxiella Burnetii Infection. Portland State University Library, 2015. http://dx.doi.org/10.15760/honors.168.

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Mozgovaya, E. E., S. A. Bedina, I. A. Zborovskaya, et al. XANTHINE OXIDOREDUCTASE AND SUPEROXIDE DISMUTASE ACTIVITIES OF BLOOD PLASMA DEPENDING ON TYPE OF SYSTEMIC SCLEROSIS. "PLANET", 2019. http://dx.doi.org/10.18411/978-5-907192-54-6-2019-xxxvi-120-127.

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สุขหร่อง, สุชาดา, та วรวุฒิ จุฬาลักษณานุกูล. โครงการ การศึกษาคุณสมบัติการกระตุ้นทางชีวภาพของน้ำหมักชีวภาพจากพืชต่อความทนทานภายใต้สภาวะเครียดจากออกซิเดชันในข้าว : รายงานวิจัยฉบับสมบูรณ์. คณะเภสัชศาสตร์ จุฬาลงกรณ์มหาวิทยาลัย, 2009. http://dx.doi.org/10.58837/chula.res.2009.3.

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งานวิจัยนี้สามารถแยกเชื้อแบคทีเรียกลุ่มที่สังเคราะห์แสงจากดินและน้ำหมักจากฟางข้าวในแปลงเกษตรอินทรีย์ได้ ซึ่งได้แก่เชื้อ Rhodopseudomanas palustris ไอโซเลทที่ 59 ที่สามารถสร้างสาร 5-aminolevulinic acid (ALA) ที่มีรายงานว่าเป็นสารที่มีประโยชน์กับพืช และนำไปใช้ในการผลิตน้ำหมักชีวภาพจากพืช โดยสามารถใช้สาร ALA นี้เป็นสารเครื่องหมาย (marker) ในการควบคุมคุณภาพของน้ำหมักชีวภาพ การเจือจางน้ำหมักชีวภาพที่ความเข้มข้น 1:500 เป็นสัดส่วนที่เหมาะสมที่สุดในการเป็นตัวกระตุ้นทางชีวภาพซึ่งทำให้ข้าวมีความสูง การเจริญเติบโต การงอก ความยาวราก และดัชนีการงอกของเมล็ดข้าวดีกว่ากลุ่มควบคุมที่ใช้น้ำเปล่า ผลของน้ำหมักชีว
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บุญ-หลง, ปรีดา. ระบบขจัด reactive oxygen species ของถั่วเหลือง (Glycine max (L.) Merrill) เมื่อได้รับความเครียดจากภาวะขาดน้ำ : รายงานวิจัย. จุฬาลงกรณ์มหาวิทยาลัย, 2007. https://doi.org/10.58837/chula.res.2007.63.

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การเปรียบเทียบการตอบสนองทางสรีรวิทยาต่อภาวะแล้งและภาวะเค็มของถั่วเหลืองพันธุ์สจ.5 และ มข.35 พบว่า ถั่วเหลืองพันธุ์ มข.35 สามารถเจริญเติบโตในภาวะแล้งได้ดีกว่าถั่วเหลืองพันธุ์ สจ.5 โดยที่ถั่วเหลืองพันธุ์ มข.35 สามารถรักษาระดับปริมาณรงควัตถุที่ใช้ในการสังเคราะห์ด้วยแสงไว้ได้ดีกว่าในช่วงที่เผชิญกับภาวะแล้ง ทั้งยังสามารถฟื้นตัวได้เร็วกว่าด้วย นอกจากนี้ ยังพบการทำงานของเอนไซม์ catalase ที่เพิ่มขึ้นอย่างมีนัยสำคัญทางสถิติทั้งในใบบริเวณยอดและใบล่างของถั่วเหลืองพันธุ์ มข.35 อย่างไรก็ตาม ในการตอบสนองต่อภาวะเค็ม พบว่า ถั่วเหลืองพันธุ์ สจ.5 มีความสามารถในการรักษาน้ำหนักแห้งต้นไว้ได้ถึง 15 วันหลังจากเผชิญก
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Bedina, S. A., E. E. Mozgovaya, I. A. Zborovskaya, A. S. Trofimenko, and E. G. Korenskaya. ENZYMATIC PROFILE OF BLOOD PLASMA IN RHEUMATOID ARTHRITIS: ACTIVITY OF XANTHINE OXIDASE, XANTHINE DEHYDROGENASE AND SUPEROXIDE DISMUTASE. Планета, 2018. http://dx.doi.org/10.18411/978-5-907109-24-7-2018-xxxv-54-61.

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Bedina, S. A., E. E. Mozgovaya, A. S. Trofimenko, S. S. Spitsina, M. A. Mamus, and E. A. Tikhomirova. ENZYMATIC PROFILE OF BLOOD PLASMA IN SYSTEMIC SCLEROSIS: ACTIVITY OF XANTHINE OXIDASE, XANTHINE DEHYDROGENASE AND SUPEROXIDE DISMUTASE. "PLANET", 2019. http://dx.doi.org/10.18411/978-5-907192-54-6-2019-xxxvi-38-45.

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Bedina, S. A., E. E. Mozgovaya, A. S. Trofimenko, et al. XANTHINE OXIDASE, XANTHINE DEHYDROGENASE AND SUPEROXIDE DISMUTASE ACTIVITIES OF BLOOD PLASMA DEPENDING ON CLINICAL FEATURES OF SYSTEMIC SCLEROSIS. Academy of Natural Knowledge, 2019. http://dx.doi.org/10.18411/1996-3955-2019-10-268-272.

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Plymate, Stephen R. Superoxide Dismutase and Transcription Factor sox9 as Mediators of Tumor Suppression by mac25 (IGFBP-rp1) in Prostate Cancer Cells. Defense Technical Information Center, 2006. http://dx.doi.org/10.21236/ada463476.

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Zilinskas, Barbara A., Doron Holland, Yuval Eshdat, and Gozal Ben-Hayyim. Production of Stress Tolerant Plants by Overproduction of Enzymatic Oxyradical Scavengers. United States Department of Agriculture, 1993. http://dx.doi.org/10.32747/1993.7568751.bard.

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Most of the objectives that were outlined in the original proposal have been met with two exceptions. Briefly, our goals were to: (1) constract transgenic tobacco plants which overproduce one or more of the enzymatic oxyradical scavengers and associated ancillary enzymes, including superoxide dismutase, ascorbate peroxidase, glutathione peroxidase, glutathione reductase, and monodehydrascorbate reductase; (2) evaluate the tolerance of these transgenic plants to oxidative stress; and (3) extend these studies to an agronomically important crop such as citrus. As can be seen i the following pages
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Pesis, Edna, Elizabeth J. Mitcham, Susan E. Ebeler, and Amnon Lers. Application of Pre-storage Short Anaerobiosis to Alleviate Superficial Scald and Bitter Pit in Granny Smith Apples. United States Department of Agriculture, 2013. http://dx.doi.org/10.32747/2013.7593394.bard.

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There is increased demand for high quality fruit produced and marketed with reduced chemical inputs to minimize toxic effects on human health and the environment. Granny Smith (GS) apple quality is reduced by two major physiological disorders, superficial scald and bitter pit (BP). These disorders cause great loss to apple growers worldwide. Superficial scald is commonly controlled by chemical treatments, mainly the antioxidant diphenylamine (DPA) and/or the ethylene action inhibitor, 1-methylcyclopropene (1–MCP). Both chemicals are ineffective in controlling bitter pit incidence. We proposed
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