• Korean Journal of Microbiology
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• v.28 no.2
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• pp.91-97
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• 1990

Complementary DNA (cDNA) coding for human cytoplasmic superoxide dismutase (SOD1) (superoxide: superoxide oxidoreductase E.C.1.15.1.1) was isolated from human liver cDNA library of $\lambda$gt11 by in situ plaque hybridization. The insery cDNA gas the 5' untranslational region (UTR) and 3'UTR of SOD1 gene. Polymerase Chain Reaction (PCR) method was used fro subcloning of SOD1 structural gene. Using synthetic sense strand primer (24mer) containing a start codon and antisense strand primer (24mer), SOD1 structural gene was selectively amplified. Amplified DNA was directly cloned into the HincII site of pUC19 plasmid. Insery cDNA was subcloned into M13 mp19 and sequenced by dideowy chain termination method with Sequenase. The nucleotide sequence of insert cDNA had an open reading frame (ORF) coding for 153 amino acid residues. The structural gene of cytoplasmic SOD was placed under the control of bacteriophage $\lambda P_{L}$ regulatory sequences, generating a highly efficient expression plasmid. The production of human SOD1 in E. coli cells was about 7% of total cellular proteins and recombinant human SOD1 possessed its own enzymatic acitivity.

• Journal of Photoscience
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• v.11 no.3
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• pp.115-120
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• 2004

For the expression study of antioxidant isoenzyme genes in rice (Oryza sativa L.) plants, extensive searches for genes of superoxide dismutase (SOD), ascorbate peroxidase (APX), and catalase (CAT) isoforms were performed through the GenBank database. The genes for two cytosolic and one plastidic CuZn-SOD, one Fe-SOD, two Mn-SOD, two cytosolic and two chloroplastic (stromal and thylakoid) APX, and three CAT isoforms were available in japonica-type rice. These isoforms were named as cCuZn-SOD1, cCuZn-SOD2, pCuZn-SOD, Fe-SOD, Mn-SOD1, Mn-SOD2, cAPXa, cAPXb, Chl_sAPX, Chl_tAPX, CATa, CATb, and CATc, respectively. Since they shared a high degree of homology in the nucleotide and amino acid sequences, the gene-specific primers for the genes were designed directly from their full-length cDNAs found in the database except for the CATa gene. These primers were used in the RT-PCR analysis to investigate the differential expression of antioxidant isoenzyme genes in rice plants from the seeds irradiated with low doses (2, 4, 8, and 16 Gy) of gamma-radiation. The gammairradiation slightly increased the transcripts of pCuZn-SOD, while those of Fe-SOD, cAPXb, and CATb decreased. However, no substantial differences were observed in the expression of all the isoenzyme genes between the control and irradiated groups. In this study, gene specific primers for thirteen SOD, APX and CAT isoenzymes were constructed from the full-length cDNAs. The results of RT-PCR analysis obtained by using these primers suggests that the expression levels of SOD, APX, and CAT isoenzyme genes in rice seedlings were hardly affected by gamma-irradiation at the seed stage.

• Proceedings of the SCSK Conference
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• 2003.09a
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• pp.630-644
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• 2003

A human Cu, Zn-superoxide dismutase (Cu, Zn-SOD) was fused with a Tat PTD of HIV-1 to produce a novel anti-aging ingredient, Tat-SOD for cosmeceuticals. Test of stability and evaluation of transduction efficacy and enzymatic activity suggest Tat-SOD is an effective active ingredient for anti-aging treatment.

• International Journal of Industrial Entomology and Biomaterials
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• v.10 no.1
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• pp.35-43
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• 2005

We describe here the complete nucleotide sequence and the exon-intron structure of the Cu,Zn superoxide dismutase (SOD1) gene of Paecilomyces tenuipes and Paecilomyces sp. The SOD1 gene of P. tenuipes spans 966 bp, and consisted of three introns and four exons coding for 154 amino acid residues. Three unambiguous introns in P. tenuipes separate exons of 13, 332, 97, and 20 bp, all exhibiting exon sizes identical to Cordyceps militaris SOD1 gene. The SOD1 gene of Paecilomyces sp. contains 946 bp and consisted of four introns and five exons coding for 154 amino acid residues. Five exons of Paecilomyces sp. SOD1 are composed of 13, 180, 152, 97, and 20 bp. Interestingly, this result showed that the total length of exons 2 (180 bp) and 3 (152 bp) of Paecilomyces sp. SOD1 is same to exon 2 length (332 bp) of C. militaris SOD1 and P. tenuipes SOD1. The deduced amino acid sequence of the P. tenuipes SOD1 showed $95\%$ identity to C. militaris SOD1 and $78\%$ to Paecilomyces sp. SOD1. Phylogenetic analysis confirmed that the C. militaris SOD1, P. tenuipes SOD1 and Paecilomyces sp. SOD1 are placed together within the ascomycetes group of fungal clade.

• Proceedings of the Botanical Society of Korea Conference
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• 1999.07a
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• pp.79-84
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• 1999

Oxidative stress is one of the major environmental stresses to plants. Reactive oxygen species (ROS) generated during metabolic processes damage cellular functions and consequently lead to cell death. Fortunately plants have in vivo defense system by which the ROS is scavenged by enzymes such as superoxide dismutase (SOD) and ascorbate peroxidase (APX). In attempts to understand the protection mechanism of plant against oxidative stress, we developed transgenic tobacco (Nicotiana tabacum cv. Xanthi) plansts thet expressed both SOD and APX in chloroplast using Agrobacterum-mediated transformation and evaluated their protection capabilities against methyl viologen (MV, paraquat) -mediated oxidative damage. Three double transformants (CAI, CA2, and CA3) expressed the chimeric CuZnSOD and chimeric APX in chloroplast, and one transformant (AM) expressed the chimeric APX and chimeric MnSOD in chloroplast. In addition, we obtained three lines of transformants (C/Al, C/A2, and A/C) that expressed the APX and SOD than control plants, and more resistant to oxidative stress caused by MV. TRansformants (C/A and A/C) overexpressing MnSOD, CuZnSOD and APX at the same time showed the highest resistance to MV-mediated oxidative stress among the transformants.

• Korean Journal of Microbiology
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• v.32 no.2
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• pp.139-146
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• 1994

Protective effects on subcellular localization of Photobacterium leiognathi CuZnSOD(PSOD) were examined in Escherichia coli SOD mutant cells on the treatment of paraquat, heat shock $(37^{\circ}C{\to}42^{\circ}C{\to})$, hydrogen peroxide and copper sulfatem respectively. The physiological characteristics of the periplasmic and cytoplasmic PSOD localized differently are dependent on the conditions in this experiment. Cells expressing SOD periplasmically in the treatments of paraquat and $H_2O_2$ respectively were somewhat better protective effects cells expressiong SOD cytoplasmically at comparable level and SOD expression level showed, the most consistently important variable. However, this was reversed in the treatments of heat shock and $CuSO_4$, respectively.

• Korean Journal of Microbiology
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• v.52 no.2
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• pp.230-235
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• 2016

This study was carried out to analyze the differences in enzyme activity and stability between the native Fe superoxide dismutase (FeSOD) and the 6xHis-tagged superoxide dismutase (6xHis-FeSOD) of Streptomyces subrutilus P5. The optimum pHs for both native FeSOD and 6xHis-FeSOD were 7, while the pH range of the activity was narrower for the 6xHis-FeSOD. The native FeSOD was stable at pH 4-9, but the 6xHis-FeSOD lost its stability at pH > 9. The temperatures of the optimum activities were same for both types of enzymes. However, the heat stability of the 6xHis-FeSOD was clearly decreased; even at $20^{\circ}C$ the enzyme lost the activity after 360 min. In contrast, the native FeSOD was stable after 720 min at below $40^{\circ}C$. $H_2O_2$ inhibition was occurred already at 0.5 mM for the 6xHis-tagged enzyme. Therefore, from the results that the 6xHis-FeSOD retained the enzyme activity at pH 6-7 and $20-40^{\circ}C$, it can be assumed that the protein structure became destabilized under different storage conditions and sensitive to the enzyme inhibitor.

• Journal of Microbiology
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• v.37 no.2
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• pp.117-122
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• 1999

Protective roles of antioxidant enzymes, copper-zinc superoxide dismutase (CuZnSOD), manganese superoxide dismutase (MnSOD), and catalase of Candida albicans against exogenous reactive oxygens and oxidative killing by macrophages were investigated. The initial growth of C. albicans was inhibited by reactive, oxygen-producing chemicals such as hydrogen peroxide, pyrogallol, and paraquat, but it was restored as the production of antioxidant enzymes were increased. The growth inhibition of C. albicans by reactive, oxygen-producing chemicals was reduced by treating the purified candidal SOD and catalase. Also, in the presence of SOD and catalase, the oxidative killing of C. albicans by macrophages was significantly inhibited. These results suggest that antioxidant enzymes, CuZnSOD, MnSOD, and catalase of C. albicans may play important roles in the protection of C. albicans not only from exogenous oxidative stress but also from oxidative killing by macrophages.

• Korean Journal of Food Science and Technology
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• v.30 no.6
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• pp.1484-1487
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• 1998

Superoxide dismutase (SOD)-like activities of sixteen kinds of fruits, vegetable juice and commercial concentrates were measured by pyrogallol autoxidation method. The changes in SOD-like activity by heat treatment and the increase in SOD-like activity of apple juice mixed with fruits and vegetables were investigated. SOD-like activity of broccoli juice was 41.7%, the highest value among tested sample. SOD-like activities of strawberry juice, carrot concentrate, kiwi juice, radish juice and apple juice were 30.2, 30.0, 27.6, 26.7, 24.1 and 14.6%, respectively. SOD-like activity was increased generally after heat treatment at $95^{\circ}C$ until 20 min. SOD-like activity of apple juice was increased $20{\sim}35%$ by mixing with 20% of carrot concentrate, kiwi juice, strawberry juice, broccoli juice, respectively and particularly was increased 48% by mixing with 20% of raddish juice.

• 한국신재생에너지학회:학술대회논문집
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• 2011.05a
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• pp.124.1-124.1
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• 2011

결정질 태양전지에서 도핑(Doping)은 반도체(Semiconductor)의 PN 접합(Junction)을 형성하는 중요한 역할을 한다. 도핑은 반도체에 불순물(Dopant)을 주입하는 공정으로 고온에서 진행되며 온도는 중요한 변수(Parameter)로 작용한다. 본 연구에서는 여러 가지 도핑 방법 중 SOD(Spin-On Dopant)를 이용하여 온도에 따른 도핑 결과와 특성을 분석 하였다. P-type 웨이퍼(Wafer)에 SOD를 이용하여 불순물을 증착 후 Hot-plate에서 15분간 Baking 하였다. Baking된 웨이퍼는 노(Furnace)에 넣고 $860^{\circ}C{\sim}880^{\circ}C$까지 $10^{\circ}C$씩 가변하였다. 각각의 조건에 대해 Lifetime과 Sheet Resistance을 측정하였고, 그 결과 $880^{\circ}C$에서의 Lifetime이 $23.58{\mu}s$로 $860^{\circ}C$에 비해 235.8% 증가하여 가장 우수 하였으며, Sheet Resistance 또한 $68{\Omega}$/sq로 $860^{\circ}C$에서 가장 우수하게 측정되었다. SOD의 속도 가변에 따른 특성 변화를 보기 위해 온도는 $880^{\circ}C$에 고정한 후 속도를 3000rpm~4500rpm까지 500rpm간격으로 1시간동안 실험한 결과 rpm 속도에 따른 lifetime 변화는 거의 없었으며, Sheet Resistance는 3000rpm에서 $63{\Omega}$/sq로 가장 우수 하였다. 본 연구를 통해 온도와 Spin rpm에 따른 특성을 확인한 결과 온도가 높을 때 Sheet Resistance가 가장 안정화 되며, lifetime이 더욱 우수한 것을 확인할 수 있었다.