• Korean Journal of Soil Science and Fertilizer
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• v.6 no.1
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• pp.27-28
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• 1973

The activities of peroxidase and polyphenoloxidase were investigated in the rice leaves(the upper halves) diseased with Akagare or Helminthosporium oryzae. The activity of polyphenoloxidase was slightly lower than that of peroxidase in the healthy leaves but it increased 56% in the diseased leaves while peroxidase decreased 35%. It was expected that polyphenoloxidase is dominant in the oxidation of polyphenols, and hydrogen peroxide may accumulate to harmful level due to the decrease of peroxidase activity resulting in non-enzymatic oxidation of polyphenols in the diseased leaves.

• Korean Journal Plant Pathology
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• v.1 no.3
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• pp.178-183
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• 1985

The present researches were carried out to investigate the peroxidase activity in association with the reactions of the 4 cultivars of rice plant, Nagdong, Jinheung, Nongbaek and Taebaek to Pyricularia oryzae race KJ-I0l and KJ-301. Although the peroxidase activity was increased during the growth of the rice seedlings, the significant difference in the activity was not found among 4 cultivars. After inoculation of the fungus, the peroxidase activity was enhanced in diseased leaves, being considerably higher in the compatible than in the incompatible cultivars. The isozyme bands of peroxidases observed in mycelium of rice blast fungus were not found in the diseased leaves on the gel electrophoresis. The peroxidase activity was not affected by the increased application of nitrogenous fertilizer.

• Proceedings of the Plant Resources Society of Korea Conference
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• 2002.11b
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• pp.67-67
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• 2002

아열대성 식물 4종 (문주란, Crinum asiaticum var. japonicum; 박달목서, Osmanthus insularis; 죽절초, Chloranthus glaber; 파초일엽, Asplenium antiquum)을 대상으로 자연 환경요인의 변화에 의한 항산화 효소 (superoxide dismutase, peroxidase, catalase, ascorbate peroxidase)의 활성과 isoenzyme 패턴의 변화를 전기영동으로 조사하였다. 그 결과, peroxidase의 활성과 isoenzyme 패턴이 식물종이나 환경조건에 따라 가장 다양하게 나타났다. Peroxidase는 4종 모두에서 여름철보다 겨울철에 활성이 높았고 문주란, 박달목서, 파초일엽에서는 겨울철에 특이적으로 발현되는 isoenzyme들도 관찰할 수 있었다. Catalase는 문주란, 박달목서, 파초일엽에서 검출되었다. 문주란 잎에서는 겨울철에 비해 여름철에 다소 높은 활성을 보였으며, 박달목서와 파초일엽에서는 겨울철에 높은 활성을 나타내었다. 그리고 문주란과 박달목서에서는 겨울철에 새벽이나 밤보다 낮시간에 높은 활성을 보였는데 파초일엽에서는 낮시간의 catalase 활성이 낮았다. Superoxide dismutase는 문주란, 박달목서, 파초일엽에서 검출되었으며, 특히 박달목서에서는 겨울철에 높은 활성을 보였다. Ascorbate peroxidase는 문주란과 파초일엽에서 관찰되었으나 계절적으로 큰 차이가 없었으며, 겨울철에는 isoenzyme 패턴의 일주기적 변화가 관찰되었다. 이상의 결과, 종별로는 문주란, 파초일엽에서 4종의 항산화효소가 모두 검출되었고, 박달목서에서는 ascorbate peroxidase가, 죽절초에서는 peroxidase를 제외한 모든 항산화 효소가 검출되지 않았다. 식물종에 따라 또는 환경요인의 변화에 따라 항산화효소의 활성 또는 isoenzyme 패턴의 차이를 보이고 있지만 항산화효소의 계절적 그리고 일주기적 변화가 관찰되어, 본 연구에서 조사된 4종의 아열대성 식물이 자연환경 조건 하에서도 산화적 스트레스에 처하고 있는 것으로 보인다.

• Applied Biological Chemistry
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• v.31 no.2
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• pp.205-210
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• 1988

The changes in peroxidase and catalase activities, and isoperoxidase patterns in different parts of mung bean seedling caused by the treatment with plant growth substances, $GA_3$ and ABA, were examined. As germination proceeded, the activity of peroxidase in all part except hypocotyl was increased, while that of catalase decreased. The separate application of $GA_3$ and ABA increased the activity of peroxidase which was more influenced by $GA_3$ than by ABA only in cotyledon, while that of catalase was more affected by ABA than by $GA_3$. Electrophoretic study revealed that the number of isoperoxidase was increased continuously in all parts during development. A greater influence was exerted on the intensity of isozyme than the number of isozyme by the hormonal treatment.

• Journal of Oral Medicine and Pain
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• v.33 no.1
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• pp.1-8
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• 2008

It is well known that many antimicrobial proteins in saliva interact with each other. The purpose of the present study was to investigate the interactions of lysozyme with peroxidase in the aspects of enzymatic activity in vitro. The interactions of lysozyme with peroxidase were examined by incubating hen egg-white lysozyme(HEWL) with bovine lactoperoxidase(bLP). The influence of peroxidase system on lysozyme was examined by subsequent addition of potassium thiocyanate and hydrogen peroxide. Lysozyme activity was determined by turbidity measurement of a Micrococcus lysodeikticus substrate suspension. Peroxidase activity was determined with an NbsSCN assay. The Wilcoxon signed rank test was used to analyze the changes of enzymatic activities compared with their controls. bLP at physiological concentrations enhanced the enzymatic activity of HEWL(P < 0.05) and its effect was dependent on the concentration of peroxidase. However, HEWL did not affect the enzymatic activity of bLP. Thiocyanate did not affect the enzymatic activity of HEWL, either. The addition of potassium thiocyanate and hydrogen peroxide did not lead to additional enhancement of the enzymatic activity of HEWL. The changes of hydrogen peroxide concentration in the peroxidase system did not affect the enzymatic activity of HEWL. Collectively, despite an in vitro nature of our study, the results of the present study provide valuable information on the interactions of lysozyme and peroxidase in the aspects of enzymatic activity in oral health care products and possibly in the oral cavity.

• The Korean Journal of Pharmacology
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• v.22 no.2
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• pp.144-150
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• 1986

Glutathione peroxidase might play an important role in the protection of cellular structures against oxidative challange by hydrogen peroxide and several organic hydroperoxides. It is widely accepted that allicin is biological active component of garlic, and allicin is easily degraded to diallyl disulfide and other components. This study was attempted to elucidate the effect of diallyl disulfide on some biological activities. It was observed that the activity of serum transaminase and glutathione level in liver were not changed by the treatment of diallyl disulfide. The liver cytosolic glutathione peroxidase activity was significantly enhanced. Whereas, mitochondrial enzyme activity was slightly increased. In the presence of diallyl disulfide in vitro, $V_{max}$ value of glutathione peroxidase for hydrogen peroxide was increased. On the other hand, Km value was not changed.

• Applied Biological Chemistry
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• v.39 no.3
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• pp.222-226
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• 1996

Lipoxygenase, peroxidase and catalase activities were determined in tissues and brines of refrigerated dill pickling cucumbers in response to pickling process, storage and $H_2O_2$. Lipoxygenase was almost inactivated within 1 day exposure to dill pickling brine, and then gradually declined during storage. In contrast, peroxidase activity in cucumber tissue decreased steadily for 4 days after exposure to dill pickling brine. Catalase was present in fresh cucumber tissues, but only slight activity was observed after submerging cucumbers in pickling brine. Lipoxygenase, peroxidase and catalase activities were rapidly inactivated in cucumbers exposed to brine containing $H_2O_2$.

• Parasites, Hosts and Diseases
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• v.30 no.4
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• pp.355-358
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• 1992

In early maturation stages of Paragonimus westermani (metacercariae, 4-, 8-, 12-week old worms), activities of antioxidant enzymes, such as superoxide dismutase, catalase, peroxidase and glutathione peroxidase, were examined. Specific activity of catalase was the highest in metacercariae and decreasing with age. That of superoxide dismutase was higher in metacercariae and 4-week worms. Specific activity of peroxidase was at its peak in 4-week worms while that of glutathione peroxidase was in 8-week worms. Specific activities of all these antioxidant enzymes were decreased to their lowest in 12-week old adults.

• KSBB Journal
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• v.23 no.4
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• pp.340-344
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• 2008

Coprinus cinereus peroxidase (CiP) was often used as a catalyst for oxidative polymerization of a variety of phenol derivatives to produce a new class of polyphenols. Economical point of view, to know the mechanism of enzyme deactivation is significantly important because cost of enzyme is critically high. Hydrogen peroxide being used as oxidizing agent induced deactivation of peroxidase by destruction of heme structure. In the presence of hydrogen peroxide the stability of peroxidase was unexpectedly improved by adding organic solvent. Especially 2-propanol significantly improved enzyme stability among tested solvents. Radical scavenging by organic solvents may play a major role in protecting peroxidase from the oxidation of oxidizing radicals.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.29 no.4
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• pp.64-72
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• 1997

백색부후균에 의한 리그닌의 분해양상을 검토하기 위해 리그닌 분해능이 우수하고 laccase활성이 높은 LKY-7 및 C. versicolor-13 균주와 manganese peroxidase 활성은 비교적 높으나 laccase활성이 전혀 나타나지 않는 LSK-27 균주로 lignosulfonate를 처리하였다. LKY-7 과 C. versicolor-13 균주에서는 lignosulfonate의 중합화 현상이 관찰되었으며 중합화는 laccase 활성 과 비례하는 것으로 나타났다. LSK-27 균주에서는 lignosulfonate의 고분자 영역이 분해되면서 탈중합화가 일어났으며 리그닌 분해 효소로는 manganese peroxidase만 검출되었다. 보조기질로 glucose를 첨가한 결과, LKY-7 균주에서는 laccase 활정이 각소하면서 중합화 현상이 어느 정도 감소하였으나 C. versicolor-13 균주는 laccase 활성의 증가와 함께 중합화도 촉진되는 것으로 나타났다. 또한 LSK-27 균주에서도 glucose 첨가에 의해 manganese peroxidase 활성이 증가되면서 lignosulfonate의 중합화가 관찰되었다. lignosulfonate 중합화에는 laccase 뿐만 아니라 manganese peroxidase도 관여하며 보조기질로서 탄소원의 종류도 영향을 미칠것으로 검토되었다.