• Title/Summary/Keyword: Fe superoxide dismutase

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Effects of Harmaline and Harmalol on the Oxidative Injuries of Hyaluronic Acid, Lipid and Collagen by $Fe^{2+}$ and $H_2O_2$ ($Fe^{2+}$$H_2O_2$에 의한 Hyaluronic Acid, Lipid와 Collagen의 산화성 손상에 나타내는 Harmaline과 Harmalol의 영향)

  • Cho, In-Sung;Shin, Yong-Kyoo;Lee, Chung-Soo
    • The Korean Journal of Pharmacology
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    • v.31 no.3
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    • pp.345-353
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    • 1995
  • ${\beta}-Carboline$ alkaloids including harmaline have been shown to inhibit enzymatically or nonenzymatically induced-lipid peroxidation of microsomes. This study was done to explore the antioxidant ability of harmaline and harmalol on the oxidative injuries of hyaluronic acid, lipid and collagen by $Fe^{2+}$ and $H_2O_2$. Their scavenging actions on reactive oxygen species were also examined. Harmaline, harmalol, superoxide dismutase, catalase and DMSO inhibited both degradation of hyaluronic acid by $Fe^{2+}$ and $H_2O_2$ and lipid peroxidation of microsomes by $Fe^{2+}$. In these reactions, DABCO inhibited degradation of hyaluronic acid but did not affect lipid peroxidation. ${\beta}-Carbolines$ inhibited degradation of cartilage collagen by $Fe^{2+}$, $H_2O_2$ and ascorbic acid. The reduction of ferricytochrome c due to autoxidation of $Fe^{2+}$, which is inhibited by superoxide dismutase, was not affected by harmaline and harmalol. They also did not have a decomposing action on $H_2O_2$. Hydroxyl radical production in the presence of $Fe^{2+}$ and $H_2O_2$ was inhibited by harmaline, harmalol and DMSO. Harmaline and harmalol may inhibit the oxidative injuries of hyaluronic acid, lipid and cartilage collagen by $Fe^{2+}$ and $H_2O_2$ through their scavenging actions on reactive oxygen species, OH and probably iron-oxygen complexes and exert antioxidant abilities.

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Characterization of Superoxide Dismutase in Lactococcus lactis

  • Chang, Woo-Suk;So, Jae-Seong
    • Journal of Microbiology and Biotechnology
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    • v.9 no.6
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    • pp.732-736
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    • 1999
  • The superoxide dismutase (SOD) in Lactococcus lactis was measured quantitatively and qualitatively under various culture conditions. The L. lactis SOD was induced by oxidative stress. As the concentration of paraquat to produce superoxide radicals increased, the growth of L. lactis decreased with concomitant increase of SOD activity. The SOD activity was found to be growth-phase dependent: when aerobically grown cells entered to the stationary phase, the activity increased gradually until the late stationary phase. From inhibition studies, L. lactis SOD was found to be insensitive to KCN and $H_2O_2$ which are known to inhibit Cu/ZnSOD and FeSOD, respectively. Moreover, as the concentration of manganese in the medium increased, the activity of SOD also increased. These data strongly suggested that L. lactis possessed a single manganese-containing SOD (MnSOD). Finally, a putative sod gene fragment of 510 bp was identified in L. lactis using a polymerase chain reaction (PCR) with degenerate primers designed from the deduced DNA sequences of known SOD genes.

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Effects of Green Tea Catechins on the Lipid Peroxidation and Superoxide Dismutase (녹차카테킨이 지질과산화 및 Superoxide Dismutase에 미치는 영향)

  • 강원식;이윤희;정현희;강민경;김택중;홍진태;윤여표
    • Journal of Food Hygiene and Safety
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    • v.16 no.1
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    • pp.41-47
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    • 2001
  • The purpose of this study was to elucidate the effects of green tea catechins (GTC) on the lipid peroxidation and superoxide dismutase (SOD). GTC showed the high SOD activity, while sitgnificantly inhibited the peroxide value of linoleic acid (93%) and lipid peroxidation (84%) from rat liver microsomal fraction induced by Fe$^{2+}$ascorbate system. The effects of GTC on the SOD and catalase activities, and lipid peroxidation after oral administration were investigated. GTC (50 mg/kg) significantly increased SOD (62%) and catalase activities (75%), while significantly inhibited the lipid peroxidation (52%) of rat liver microsome in a dose-dependent manner. These results suggest that GTC has the antioxidative effect which is rotated to the prevention of aging and cancer.r.

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Effect of Metal Ions on Speroxide Dismutase of the Liver in Senescence-Accelerated Mouse(SAM) (노화촉진생쥐(SAM)의 간에서 금속이온이 SOD의 활성에 미치는 영향)

  • 양미경;박문숙
    • Journal of environmental and Sanitary engineering
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    • v.15 no.2
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    • pp.1-9
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    • 2000
  • This research employed a senescence-accelerated mouse(SAM) to explore the possibility that differences exits among the major antioxidants, superoxid dismutase(SOD), in terms of ability to protect such animal treated with Cu, Fe and Mn. To assess the antioxidants function of metal ions on SAM-R/1 and SAM-P/8 were administered with Cu, Fe and Mn orally. The effect of metal ions on SAM towards reversing oxygen sensitivity was determined as a bioassays of SOD in the mouse liver. The data show that the SOD activity was induced by each metal ions in both SAM-R/1 and SAM-P/8. It suggested that induced SOD by each metal ions may protect against oxidative mediated stress. Finally, overall data lead to the possibility of metal ions as an antioxidants or each metal ions act producer of oxygen radicals in the liver of SAM-R/1 and SAM-P/8.

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The Virulence of Vibrio vulnificus is Affected by the Cellular Level of Superoxide Dismutase Activity

  • Kang, In-Hye;Kim, Ju-Sim;Lee, Jeong-K.
    • Journal of Microbiology and Biotechnology
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    • v.17 no.8
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    • pp.1399-1402
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    • 2007
  • The virulence of superoxide dismutase (SOD) mutants of Vibrio vulnificus, as tested by intraperitoneal injection into mice, decreases in the order of sodC mutant, sodA mutant, and sodB mutant lacking CuZnSOD, MnSOD, and FeSOD, respectively. The survival of SOD mutants under superoxide stress also decreases in the same order. The virulence of soxR mutant, which is unable to induce MnSOD in response to superoxide, is similar to that of the sodA mutant, as the survival of the soxR mutant under superoxide stress is similar to that of the sodA mutant. Consistently, the lowered survival of the soxR mutant is complemented not only with soxR but also with sodA. Thus, the virulence of V. vulnificus is significantly affected by the cellular level of SOD activity, and an increase in SOD level through MnSOD induction by SoxR under superoxide stress is essential for virulence.

An Efficient Method for the Expression and Reconstitution of Thermostable Mn/Fe Superoxide Dismutase from Aeropyrum pernix K1

  • Lee, Hee-Jin;Kwon, Hye-Won;Koh, Jong-Uk;Lee, Dong-Kuk;Moon, Ja-Young;Kong, Kwang-Hoon
    • Journal of Microbiology and Biotechnology
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    • v.20 no.4
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    • pp.727-731
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    • 2010
  • The gene APE0743 encoding the superoxide dismutase (ApSOD) of a hyperthermophilic archaeon Aeropyrum pernix K1 was cloned and overexpressed as a GST fusion protein at a high level in Escherichia coli. The expressed protein was simply purified by the process of glutathione affinity chromatography and thrombin treatment. The ApSOD was a homodimer of 25 kDa subunits and a cambialistic SOD, which was active with either Fe(II) or Mn(II) as a cofactor. The ApSOD was highly stable against high temperature. This thermostable ApSOD is expected to be applicable as a useful biocatalyst for medicine and bioindustrial processes.

Cu,Zn-Superoxide Dismutase Is an Intracellular Catalyst for the H2O2-dependent Oxidation of Dichlorodihydrofluorescein

  • Kim, Young-Mi;Lim, Jung-Mi;Kim, Byung-Chul;Han, Sanghwa
    • Molecules and Cells
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    • v.21 no.1
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    • pp.161-165
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    • 2006
  • Dichlorodihydrofluorescein ($DCFH_2$) is a widely used probe for intracellular $H_2O_2$. However, $H_2O_2$ can oxidize $DCFH_2$ only in the presence of a catalyst, whose identity in cells has not been clearly defined. We compared the peroxidase activity of Cu,Zn-superoxide dismutase (CuZnSOD), cytochrome c, horseradish peroxidase (HRP), $Cu^{2+}$, and $Fe^{3+}$ under various conditions to identify an intracellular catalyst. Enormous increase by bicarbonate in the rate of $DCFH_2$ oxidation distinguished CuZnSOD from cytochrome c and HRP. Cyanide inhibited the reaction catalyzed by CuZnSOD but accelerated that by $Cu^{2+}$ and $Fe^{3+}$. Oxidation of $DCFH_2$ by $H_2O_2$ in the presence of a cell lysate was also enhanced by bicarbonate and inhibited by cyanide. Confocal microscopy of $H_2O_2$-treated cells showed enhanced DCF fluorescence in the presence of bicarbonate and attenuated fluorescence for the cells pre-incubated with KCN. Moreover, DCF fluorescence was intensified in CuZnSOD-transfected HaCaT and RAW 264.7 cells. We propose that CuZnSOD is a potential intracellular catalyst for the $H_2O_2$-dependent oxidation of $DCFH_2$.

Purification and Characterization of Superoxide Dismutase from Pseudomonas polycolor

  • LEE SANG-OK;IL-CHUN SEO;SOOK-HYUN CHUNG;TAE-HO LEE
    • Journal of Microbiology and Biotechnology
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    • v.3 no.3
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    • pp.188-193
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    • 1993
  • Superoxide dismutase (SOD) was purified from Pseudomonas polycolor to an electrophoretically homogeneous state and partially characterized. SOD was purified by ammonium sulfate fractionation, column chromatography on DEAE-Sephadex A-50, phenyl-Toyopearl 650 M, and gel filtration on Sephadex G-100. The molecular weight and subunit molecular weight of the purified enzyme were estimated to be 40, 000 and 20, 000, respectively. The purified enzyme remained stable at pH 9.0~11.0, $25^{\circ}C$ for 40 hr, but rapidly became inactive below 9.0. SOD was stable up to $45^{\circ}C$ at pH 9.0 with about 80% relative activity, but rapidly became inactive at temperature above that. The enzyme was insensitive to cyanide and fluoride, and sensitive to hydrogen peroxide and azide. The results suggest that the enzyme be an iron-containing SOD.

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Effects of Dietary Cheongkukjang on Liver Superoxide Dismutase Activity of Parrotfish Oplegnathus fasciatus (사료 내 분말 청국장이 돌돔, parrootfish, Oplegnathus fasciatus의 간 내 superoxide dismutase 활성에 미치는 영향)

  • Pham, Minh Anh;Lee, Kyeong-Jun
    • Journal of Aquaculture
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    • v.20 no.2
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    • pp.132-139
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    • 2007
  • A four-week feeding trial was conducted to investigate the effects of dietary soybean meal (SBM) and powdered Cheongkukjang (CKJ) on non-specific immune responses of parrotfish Oplegnathus fasciatus. Three isonitrogenous (42% crude protein) and isocaloric (17.1 MJ/kg) diets were formulated to replace fish meal by 0, 25% SBM or 25% CKJ (designated as FM, 25SBM and 25CKJ, respectively). Ninety fish (initial body weight 122 g) were randomly allotted into nine 150 L tanks. One of the three experimental diets was fed to triplicate groups of fish for 4 weeks. After the feeding trial, no differences were observed in growth performances and feed utilization among fish groups. Liver superoxide dismutase activity of the fish fed CKJ containing diet was significantly higher than that of the control groups. DPPH radical scavenging and $Fe^{2+}-chelating$ activities of the experimental diets containing SBM or powdered CKJ were significantly higher than that of the control diet. The results of the present study suggest that dietary inclusion of powdered 25CKJ significantly increased liver superoxide dismutase activity and did not affect the growth performances, feed utilization, morphological parameters, as well as hematological values of parrotfish.

Activity of Superoxide dismutase(SOD) by fermented soybean (발효 대두 식품의 Superoxide dismutase(SOD) 활성)

  • 류병호;박종옥;김의숙;임복규
    • Journal of Life Science
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    • v.11 no.6
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    • pp.574-581
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    • 2001
  • This study was performed to evaluate the inhibition effects of fermented soybean on lipid perosidation and antioxidative relative enzyme activity. in vivo. Fermented soybean was induced the high SOD activity, while significantly inhibited on the peroxide value of linoleic acid and lipid perxidation from rat microsome induced by Fe$^{2+}$ ascorbate system, Sprague-Dawley(SD) male rats were fed basic diet, and experimental diets group added 200 or 500 mg/kg fermented soybean for 2 weeks. The effect of fermented soybean is also significantly increased catalase and glutathione peroxidase activities, while significantly inhibited the lipid peroxidation of rat liver microsome in a dose dependent manner. Therefore, these results suggest that fermented soybean has antioxidative activity which is related enzyme to prevention of oxidative stress.s.

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