• Journal of the Korean Society of Food Science and Nutrition
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• v.19 no.3
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• pp.224-228
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• 1990

Cabbage contained high peroxidase activity among tested plant sources. The cabbage peroxi-dase can replace horseradish peroxidase to assay glucose with glucose oxidase. The amount of glucose can be determined quantitatively by glucose oxidase-cabbage peroxidase. The opti-mum pH and temperature for enzymatic glucose determination by glucose oxidase-cabbage peroxidase were 6.0 and 35-45$^{\circ}C$ respectively. The glucose assay was inhibited by addition of various metal salts such as mercuric chloride lead acetate silver nitrate ammonium molyb-date sodium tunstate and cupric sulfate. The relationship between absorbance and amount of glucose was linear up to 8.33 mM glucose in the assay mixture under the assay conditions.

• Journal of Oral Medicine and Pain
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• v.33 no.3
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• pp.229-240
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• 2008

Animal mucins have structural characteristics similar to human salivary mucins. Animal mucins have been regarded as suitable substances for saliva substitutes. Since animal mucin molecules in saliva substitutes and host-derived antimicrobial salivary molecules exist simultaneously in whole saliva and the pellicles of patients with dry mouth, interactions may occur between these molecules. The purpose of this study was to investigate the influence of animal mucins on peroxidase activity in solution and on the surface of hydroxyapatite(HA) surfaces. The effects of animal mucins on peroxidase activity were examined by incubating porcine gastric mucin(PGM) or bovine submaxillary mucin (BSM) with either bovine lactoperoxidase(bLPO) or saliva samples. For solid-phase assays, immobilized animal mucins or peroxidase on three different HA surfaces(HA beads, HA disc, and bovine tooth) were used. Peroxidase activity was determined with an NbsSCN assay. The obtained results were as follows: 1. PGM enhanced the enzymatic activity of bLPO in solution phase. PGM did not affect the enzymatic activity of peroxidase in saliva sample(POS). 2. BSM did not affect the enzymatic activities of both bLPO and POS in solution phase. 3. HA-adsorbed PGM increased subsequent bLPO adsorption in all three HA phases. The activity of POS was increased on both the HA beads and bovine tooth. 4. The peroxidase activities on the HA beads and disc were increased when the HA surfaces were exposed to a mixture of bLPO and PGM. 5. The binding affinity of bLPO to PGM was greater than that of bLPO to BSM. Collectively, our results suggest that animal mucins affects the enzymatic activity of peroxidase on the HA surfaces as well as in solution. Saliva substitutes containing animal mucins may affect the function of antimicrobial components in natural saliva and saliva substitutes.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.28 no.3
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• pp.374-378
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• 1983

As one way of evaluating polymorphism in maize, variation of peroxidase 8 (Px.8) in maize plants was investigated by means of horizontal acrylomide electrophoresis. The specific part of maize plants was stele and other parts of plants were also studied for 34 different maize lines and hybrids. The results obtained indicate that Px.8 has three distinct migrating patterns on gel such as fast, slow and fast-slow. The band pattern varied with materials used. Most hybrids were showing fast-slow band, indicating that those hybrids are heterozygous at least for Px.8 allele. Variation of band pattern was obseerved within a single inbred line. The Px.8 in stele tissue and in young leaf and nodal tissue was found to be identical, indicating the possible use of those tissues as an alternative tissue for Px.8 study. It was also found that there might be some definite relationship between Px.8 and Px.3 activities in the same tissue.

• The Korean Journal of Zoology
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• v.29 no.2
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• pp.141-158
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• 1986

A glutathione peroxidase from white rat (Wistar strain)erythrocytes was partially purified and characterized. In addition, localization of this enzyme in the liver was studied by histochemical method. A glutathione peroxidase was purified approximately 33.5-folds by ammonium sulfate precipitation, Sephadex filtration column and DEAE-Sephadex column chromatography. The optimum temperature of the crude glutathione peroxidase was $40^\\circC$, and the optimum pH was 7.5. This crude glutathione peroxidase was most stable at $30^\\circC$ and the values of Km and Vmax were calculated to be 8.5mM and 15.6 $\\mu$moles/min for glutathione, and 40 $\\mu$M and 10.5 $\\mu$moles/min for hydrogen peroxide, respectively. The molecular weight of this enzyme was estimated by Sephadex G-200 gel filtration to be approximately 90, 000. By electron microscopic examination, histochemical reaction products were microbodies that were prominent in the peripheral parts of the lobule. The reaction products exhibited round shapes, the diameter of which varied $0.2\\sim0.7 \\muM$ and their boundary membranes were not distint.

• Journal of radiological science and technology
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• v.15 no.1
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• pp.123-130
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• 1992

This study was prepared to observe the change of enzyme activities in kidney treated with red ginseng extract in the gamma ray irradiated mice. Determine the activity of SOD, peroxidase, catalase in the kidney a period of 1 day, 2 day, 3 day, 4 day, 5 day after a saline injection or injection of red ginseng extract or gamma ray irradiatied group into four classify. The activity SOD and catalase showed a tendency to increase and recovery at the early state but pay no regard. Wherease, the activity of peroxide restored and increased pay regard. A physiological saline injection group after gamma ray irradiation showed a tendency to diminish after remakable increase of activity of SOD, peroxidase and catalase than control group. Injection group of red ginseng extract after gamma ray irradiation observed rapid recovery on activity of SOD, peroxidase, catalase than a saline injection group. Experimental result suggested that injection of red ginseng extract after irradiation have the recovery effect on the changed of activity of SOD, peroxidase and catalase against radiation injury.

• Korean journal of applied entomology
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• v.21 no.1 s.50
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• pp.23-26
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• 1982

The present study was carried out to investigate the change of peroxidase activity of soybean seed infected with Cerrospora kikurhii. The protein content, polyphenol oxidase activity and peroxidase isozyme pattern in health and infected soybean seed were also compared. 1. The peroxidase activity was substantially higher in the infected soybean seeds than that in the healthy seeds either cracked or not. No significant differences in protein content were recognized among the seeds tested. 2. No significant differences in peroxidase activities and protein contents were notified between healthy and infected seeds from the measurements on each parts of dissected seeds, cotyledon and seedcoat, however the peroxidase activity in the seed coat of the stained seed was 2.5 times to healthy seed. 3. The activities of polyphenel oxidase were undectable in both healthy and diseased seeds. 4. The electrophoretic Patterns of the Peroridase isozyme were the same between healthy and in footed seed. 5. Therefore, the increase of peroxidase activity in infected soybean seedcoat was mainly due to the biochemical reaction against the pathogen.

• Journal of Oral Medicine and Pain
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• v.39 no.3
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• pp.90-95
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• 2014

Purpose: To investigate viscosity and wettability of hyaluronic acid (HA) solutions according to supplementation of lysozyme and/or peroxidase, and different ionic strength and pH conditions. Methods: Solutions containing HA were prepared using distilled deionized water (DDW) and simulated salivary buffer (SSB) in different conditions. Different concentrations of hen egg-white lysozyme and bovine lactoperoxidase was added into HA solutions. HA solutions with antimicrobials in different ionic strength and pH conditions were prepared. Viscosity was measured using cone-and-plate digital viscometer at six different shear rates and wettability on acrylic resin and Co-Cr alloy was determined by contact angle. Results: The viscosity values of HA dissolved in DDW were decreased in order of HA, HA containing lysozyme, HA containing peroxidase, and HA containing lysozyme and peroxidase. The viscosity values for HA in DDW were decreased as the concentration of lysozyme and/or peroxidase increased. However, the viscosity values for HA in SSB showed no significant changes according to the concentration of lysozyme and/or peroxidase. The viscosity values of HA solutions were inversely proportional to ionic strength and pH. The contact angle of HA solutions showed no significant differences according to tested surface materials, addition of lysozyme and/or peroxidase, and different ionic strength and pH conditions. Contact angles on acrylic resin by HA solutions in all tested conditions were much higher than those by human saliva. Conclusions: The rheological properties of HA supplemented with lysozyme and/or peroxidase in different ionic strength and pH conditions were objectively confirmed, indicating the possibility of HA with lysozyme and/or peroxidase as main components in the development of effective saliva substitutes.

• Korean Journal of Food Science and Technology
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• v.37 no.6
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• pp.951-956
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• 2005

Selection of oxygen-tolerant strains and elucidation of their oxygen tolerance mechanism were crucial for effective use of bifidobacteria. Oxygen-tolerant bifidobacteria were able to significantly remove environmental oxygen (oxygen removal activity) as compared to oxygen-sensitive strains. Most oxygen removal activity was inhibited by heat treatment and exposure to extreme pH (2.0) of bifidobacterial cell. NADH oxidase was major enzyme related to oxygen removal activity. Oxygen-tolerant bifidobacteria possessed high NADH peroxidase activity level to detoxify $H_2O_2$ formed from reaction of NADH oxidase. Addition of oxygen to anaerobic culture broth significantly increased activities of HADH oxidase and NADH peroxidase within 1hr and rapid increment of oxygen concentration was prevented. Results showed NADH oxidase and NADH peroxidase of oxygen-tolerant bifidobacteria played important roles in elimination of oxygen and oxygen metabolite $(H_2O_2)$.

• The Journal of Natural Sciences
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• v.14 no.1
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• pp.7-24
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• 2004

We found new type of thiol peroxidase, fused with GRX.(TPx-GRX) The TPx-GRX exists in pathogenic bacteria including -. This protein was homogeneously purified from the E.coli recombinant overexpressing TPx-GRX. In the presence of a thiol-containing electron donor such as DTT, the purified TPx-GRX has potent the antioxidant to prevent the inactivation of GS by the MCO system, which is comprised of DTT, $Fe^{3+}$, and $O^2$. The antioxidant activity is much higher that other thiol peroxidase. The investigate the peroxidase activity of TPx-GRX, we directly measured the peroxidase activity of TPx-GRX toward peroxides in terms of the removal of peroxides in the presence of GSH. This result demonstrates that the peroxidase activity of TPx-GRX. These taken together results suggest that TPx-GRX is a new member of thiol peroxidase. These observations also suggest that in the pathogenic bacteria, TPx-GRX plays an important antioxidative role as a multiple array defence mechanism against oxidative stress.

• 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 $H_2O_2$.