• Proceedings of the Zoological Society Korea Conference
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• 1996.10a
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• pp.182.2-182
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• 1996

• Korean Journal of Environmental Agriculture
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• v.36 no.4
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• pp.256-262
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• 2017

BACKGROUND: Seed of perilla (Perilla frutescens var. japonica Hara) is short-lived in conventional storage conditions. For long-term conservation of plant species, cryopreservation is the method currently available. This study was performed to find out reliable methods for a long-term storage of seeds of perilla as a genetic resource. METHODS AND RESULTS: Using seeds of 9 perilla cultivars, the effects of desiccation, aging, and cryopreservation on seed germinability and ascorbate peroxidase activity in the seeds were investigated. Initial germinability of the seeds was various, and dry seeds of all cultivars survived cryopreservation without loss of viability. The highest germination was achieved at 4-5% moisture content, and stimulatory effect of cryogenic temperature on the seed germination was observed in some cultivars. Accelerated aging of perilla seeds led to reduction in germination and ascorbate peroxidase activity, and the susceptibility of seeds to aging was different among the tested cultivars. No significant difference in germination was observed for the aged seeds of control and liquid nitrogen exposed. CONCLUSION: The results of this study suggest that cryopreservation at 4-5% moisture content would be a suitable method for long-term conservation of perilla seeds without detrimental effects on germination.

• Proceedings of the Korean Society of Grassland Science Conference
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• 2002.09a
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• pp.17.2-18
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• 2002

• Applied Biological Chemistry
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• v.43 no.1
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• pp.46-51
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• 2000

The resistance of Cornyza bonariensis to herbicide paraquat was investigated by evaluating the activities of three enzymes concerning in scavenging paraquat-generated toxic oxygen species such as superoxide radical and hydrogen peroxide in resistant and susceptible biotypes. Conyza bonariensis inhabited in cultivated area was more tolerant to paraquat than that of uncultivated area. This is the first report that a biotype of Cornyza bonariensis has appeared in an area with repeated paraquat treatments of Korea. Superoxide dismutase activity of resistant biotype was 20% higher as 150 than that of susceptible biotype. Ascorbate peroxidase activity of resistant biotype was 44% higher than that of susceptible biotype. Glutathione reductase activity of resistant biotype was 64% higher than that of susceptible biotype. It can be concluded from above results that the resistance of Conyza bonariensis to paraquat depends partially on the toxic oxygen species-scavenging efficiency of protective multienzymatic system which is composed of three enzymes, superoxide dismutase, ascorbate peroxidase, and glutathione reductase.

• Horticultural Science & Technology
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• v.18 no.6
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• pp.783-786
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• 2000

This study was carried out to examine the effect of root-zone temperatures on seedling growth, mineral contents and antioxidative enzyme activities of grafted watermelon. The grafted watermelon seedlings were grown in greenhouse bed for 20 days at root-zone day temperatures of 10, 15, $25^{\circ}C$ while night temperature was maintained at $10^{\circ}C$. Growth such as shoot height, leaf length, leaf number, stem diameter, and fresh and dry weights increased as increasing root-zone temperatures, and leaf area with $25^{\circ}C$($52.79mm^2$) was two times that of control($21.50mm^2$). As increasing the root-zone temperatures, Mn, Ca, Fe contents increased, K, P, Mg were non significant, and Na decreased. The activities of ascorbate peroxidase(APX) and guaiacol peroxidase(GPX) known as antioxidative enzyme were higher at $10^{\circ}C$ than $25^{\circ}C$.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.50 no.4
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• pp.286-290
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• 2005

Ascorbate peroxidase (APX) plays a crucial role in the detoxification of hydrogen peroxide. APX activity is maintained significantly higher in the paraquat­treated leaves of the paraquat-tolerant Rehmannia glutinos. This study was conducted to understand structural and regulatory characteristics of APX gene in R. glutinosa. A putative APX cDNA clone (RgAPX1) was isolated from a leaf cDNA library using a partially sequenced expressed sequence tag clone. RgAPX1 is consisted of 1148 bp nucleotides and contains an open reading frame encoding a 250 amino acid-long polypeptide. Deduced RgAPX1 amino acid sequence shares higher sequence similarity to cytosolic APXs. RgAPX1. expression was higher in the leaf than in the flower and root. Southern blot result indicates the presence of one or two RgAPX1-related genes in R. glutinosa genome. RgAPX1 transcription was affected differentially by various stresses and phytohormone. The results indicate that RgAPXl is constitutively expressed in most tissues and its expression is modulated for the immediate and efficient detoxification of $H_2O_2$ under normal and stress conditions.

• Journal of Environmental Science International
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• v.10 no.1
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• pp.79-84
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• 2001

To assess resistance of transgenic tobacco plants which overexpress superoxide dismutase (SOD) and ascorbate peroxidase (APX) in chloroplasts to water stress, changes in leaf water potential, turgor potential, stomatal conductance and transpiration rate were measured. Leaf water potential in all plants remained high up to day 4 after withholding water but thereafter decreased markedly. In spite of a remarkable decrease in leaf water potential, some of transgenic plants maintained higher turgor potential compared with control plant on day 12. In particular, the transgenic plant expressing MnSOD showed an outstanding maintenance in turgor pressure by osmotic adjustment throughout the experiment, resulting in high stomatal conductance and transpiration rate. However, among transgenic plants, osmotic potential was reduced more effectively in multiple transformants such as the double transformant expressing both MnSOD and APX, and the triple transformant expressing CuznSOD, MnSOD and APX than single transformants. Consequently, further research is needed to get general agreement on the tolerance of transgenic plants to water stress at different growth stages for each transgenic plant.

• Journal of Ginseng Research
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• v.24 no.3
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• pp.113-117
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• 2000

To analyze the correlation between the rusty root and the antiokidative activity in ginseng (Panax ginseng C.A.Meyer) roots, the levels of antioxidative activity in various tissues of healthy and rusty roots. The superoxide dismutase activity in rusty roots (126.9 units/mg protein) was approximately 3.5 times higher than that in healthy roots. The catalase activity in rusty roots was approximately 1.6 times higher than that in healthy roots, whereas the peroxidase activity showed a slight low level in msty roots. The 1.1 diphenyl-2-picryl-hydrazyl(DPPH) free radical scavenging activity in rusty roots was approximately 2.0 times higher than that in healthy roots. The total ascorbate content in healthy roots was 166~240 $\mu\textrm{g}$/g fr. wt. depending on the tissues. Interestingly, the oxidized dehydroascorbate (DHA) content occupied more than 80% in total ascorbate content. The total ascorbate content in rusty roots was a similar level with healthy roots, but the reduced ascorbate content was 3.5~7.5 times higher than that of the healthy roots. The total glutathione content of the epidermis, cortex and stele tissues in 겨sty roots was 7.3, 4.8, 1.2 times higher than the healthy tissues, respectively. The ratio of reduced glutathione (GSH) and oxidized glutathione (GSSG) showed a similar fluctuation of total glutathione content in 겨sty roots. These results indicate that the high antioxidative activity in rusty roots may involve in overcoming the oxidative stress derived from environmental stresses.

• Molecules and Cells
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• v.39 no.1
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• pp.20-25
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• 2016

Photosynthesis is a highly robust process allowing for rapid adjustment to changing environmental conditions. The efficient acclimation depends on balanced redox metabolism and control of reactive oxygen species release which triggers signaling cascades and potentially detrimental oxidation reactions. Thiol peroxidases of the peroxiredoxin and glutathione peroxidase type, and ascorbate peroxidases are the main peroxide detoxifying enzymes of the chloroplast. They use different electron donors and are linked to distinct redox networks. In addition, the peroxiredoxins serve functions in redox regulation and retrograde signaling. The complexity of plastid peroxidases is discussed in context of suborganellar localization, substrate preference, metabolic coupling, protein abundance, activity regulation, interactions, signaling functions, and the conditional requirement for high antioxidant capacity. Thus the review provides an opinion on the advantage of linking detoxification of peroxides to different enzymatic systems and implementing mechanisms for their inactivation to enforce signal propagation within and from the chloroplast.

• Korean Journal of Soil Science and Fertilizer
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• v.46 no.1
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• pp.32-39
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• 2013

The relationship between relative water contents of lettuce leaves and biochemical activities in lettuce was examined in this study to explore an adaptation response of lettuce to water stress from soils. Soil water contents and relative water contents of leaves were positively related to show $R^2$=0.8728. Hydrogen peroxide contents of leaves rapidly increased with reduction of soil water content, whereas soluble protein contents and dry matters rapidly decreased. And chlorophyll a and b contents of leaves decreased with increase in carotenoid content. Furthermore, the activities of ascorbate peroxidase (APX), monodehydroascorbate reductase (MDHAR), and dehydroascorbate reductase (DHAR) increased dramatically, and mRNA transcript levels of APX, MDHAR and DHAR also increased. Relationship of relative water content of lettuce leaves to hydrogen peroxide, to ascorbate peroxidase activity, to dehydroascorbate reductase activity, and to monodehydroascorbate reductase activity was shown to be positively correlated. It is highly plausible from this study that these enzyme activities could be developed as an indicator of water states in soils.