• Applied Biological Chemistry
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• v.35 no.4
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• pp.276-280
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• 1992

Quantutative analysis of catechins by HPLC was studied. When the mobile phase was switched from the conventional(AOAC) Methanol, Acetonitril and Acetic acid solution in $H_2O$ to 0.06% Phosphate solution with Acetonitrile, N,N-Dimethyl formamide, and Ethyl acetate, retention time could be reduced from 45 min to 28 min, especially, we obtained sharper chromatogram of the compounds, either (-)EGCG or (-)ECG, which resulted in minimization of analytical erros. CVs of retention time $(0.32{\sim}3.97%)$ and peak area $(1.61{\sim}7.01%)$ indicated that the data were more reliable. Content of catechins in commerical teas analyzed by the method was $120.3{\sim}153.7\;mg/g$ in green teas which was about 4 times that in black tea.

• Journal of the Korean Society of Food Science and Nutrition
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• v.20 no.3
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• pp.260-265
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• 1991

The effective method to detect the mutagenicity of N-nitrosodimethylamineI (NDMA) by using Salmonella/microsome assay was studied. The Effect of vitamin C on the mutagenicity of the formed NDMA and during the formation of NDMA from nitrite and secondary amine was also investigated. Aroclor 1254-induced hamster S9 mix was more effective in activation NDMA than rat S9 mix induced by Aroclor 1254 or phenobarbital. Dimethyl sulfoxide and ethanol suppressed the mutagenic effect of NDMA, however, phosphate butter (pH 7.4), distilled water, 95% methanol and Tween 80 + water (1 : 4) were the appropriate dissolving system in the mutagenicity test of NDMA. Vitamin C did not show any inhibitory effect on the mutagenicity of the formed NDMA. However, the revertants of Salmonella typhinutrium TA 100 were significntly reduced (p<0.05) when vitamin C was added to the reaction mixture of nitrite and dimethylamine during the formation of NDMA. The amount of the formed NDMA was analyzed using HPLC and the level was decreased by about 95%. Thus it was concluded that vitamin C inhibited greatly the formation of NDMA from nitrite and dimethylamine.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.27 no.1
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• pp.17-27
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• 2001

A cell-based assay system for monitoring NF-$textsc{k}$B activity was developed to determine the influence of activated NF-$textsc{k}$B in human HaCaT cells. The pNF-$textsc{k}$B-SEAP-NPT plasmid that permits expression of the secreted alkaline phosphatase (SEAP) reported gene in response to the NF-$textsc{k}$B activity and contains neomycin phosphotransferase (NPT) gene for the geneticin resistance in host cells was constructed and transfected into human keratinocyte cell line HaCaT. Human HaCaT transfectant cells secreted the SEAP enzyme into the culture medium in a time-dependent manner until 72h. NF-$textsc{k}$B activities were measured in the SEAP reporter gene assay using a fluorescent detection method. The treatment of HaCaT cell transfectants with known antioxidants [e.g., N-acetyl-L-cysteine and vitamin C] showed inhibition of NF-$textsc{k}$B activity in a time-and concentration-dependent manner. The phorbol 12-myristate 13-acetate (PMA) known as a stimulator of NF-$textsc{k}$B expression demonstrated that it increased NF-$textsc{k}$B activity in a time- and concentration-dependent manner. This assay system could be used to determine the quantitative measurement of NF-$textsc{k}$B activity in the human skin and allow the screening of anti-inflammatory agents from various synthetic chemicals and natural products for dermatological purpose. Abbrevitions used: NF-$textsc{k}$B, nuclear factor kappa B; I-$textsc{k}$B, Inhibitory kappa B; SEAP, secreted alkaline phosphatase; NPT, neomycin phosphotransferease; PCR, polymerase chain reaction: dNTP, deoxynucleoside triphosphates; DMEM, dulbecco’s modified eagle medium; FBS, fetal bovine serum; PBs, phosphate-buffered saline; MUP, 4-methylumbellifery phosphate; NAC, N-acetyl-L-cysteine; DMSO, dimethyl sulfoxide; PMA, phorbol 12-myristate 13-acetate.

• Journal of Food Hygiene and Safety
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• v.15 no.2
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• pp.144-150
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• 2000

The present study was peformed to determine the hydrolysis rate constants and degradation products of phosphamidon and proffnofos by the OECD method. Hydrolysis rate constants of phosphamidon in pH 4, pH 7, and pH 9 buffer solutions at 25 and 40$^{\circ}$C were 0.0020, 0.0022, 0.0049 and 0.0040, 0.0050, 0.0150, respectively. Hydrolysis rate of phosphamidon was accelerated by temprerature change under same pH conditions, and half-life of phosphamidon in pH 9 at 40。C was 3 times faster than that at 25。C. Hydrolysis rate of phosphamidon in alkaline solution(pH 9) was 2~4 times faster than that in acidic solution(pH 4) and neutral solution(pH 7) under same temperature. Hydrolysis rate constants of profenofos in pH 4, pH 7, and pH 9 buffer solutions at 25 and 40。C were 0.0022, 0.0047, 0.0860 and 0.0035, 0.0086, 0.1245, respectively. Hydrolysis rate of profenofos was accelerated by temprerature change under same pH conditions. Hydrolysis rate of profenofos in alkaline solution(pH 9) was 15~40 times faster than in acidic solution(pH 4) and neutral solution(pH 7) under same temperature condition, and half-life of profenofos was very fast within 8 hours. The hydrolysis rate of profenofos was faster than that of phosphamidon. In order to identify hydrolysis products, the extracts of degradation products were analyzed by GC/MS. The mass spectra of hydrolysis products of phosphamidon were at m/z 153 and 149, those of the profenofos were at m/z 208 and 240, respectively. The hydrolysis products of phosphamidon were O, O-dimethyl phosphate(DMP) and N, N-diethylchloroacetamide, and those of profenofos were 4-bromo-2-chlorophenol and O-ethyl-S-propyl phosphate.

• Toxicological Research
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• v.6 no.1
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• pp.109-119
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• 1990

Ro09-0198, a cyclic peptide isolated from culture filtrates of Streptoverticillium griseoverticillatum, induced lysis of erythrocytes. Ro-09-0198-induced hemolysis was temperature-dependent and the sensitivity of hemolysis differed greatly among animal species. Preincubation of the peptide with phosphatidylethanolamine reduced the hemolytic activity, whereas other phospholipids present in erythrocytes in nature had no effect. A study of the structural requirements on phosphatidylethanolamine necessary for interaction with the peptide indicates that Ro09-0198 recognizes strictly a particular chemical structure of phosphatidylethanolamine: dialkylphosphoethanolamine as well as 1-acylglycerophosphoethanolamine showed the same inhibitory effct on hemolysis induced by Ro09-0198 as diacylphosphatidyl-ethanolamine, whereas phosphoethanolamine gave no inhibitory effect. Neither phosphatidyl-N-monomethylethanolamine nor alkylphosphopropanolamine had an inhibitory effect. Proton resonances of the peptide were observed in dimethyl sulfoxide solution in the presence of 1-dodecanoyl-sn-glycerophosphoethanolamine. This peptide caused permeability increase and aggregation of liposomes containing phosphatidylethanolamine. A glycerol backbone and a primary amino group of phosphatidylethanolamine are necessary for interaction with Ro09-0198 to cause membrane damage. Ro09-0198 induced a selective permeability change on liposomes. Glucose and umbelliferyl phosphate were effluxed significantly, but sucrose was only slightly permeable and inulin could not be released. Platelet aggregation and serotonin release simultaneously induced by Ro09-0198. Addition of peptide to rat platelet, loaded with the fluorescent $Ca^{++}$ chelator quin-2, caused immediate rise in cytosolic free $Ca^{++}$ to liposomal membrane containing phosphatidylethanolamine was observed dose dependently.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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• pp.815-822
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• 1993

This experiment was carried out to determine the separation condition of 1-dimethylaminonaphthalene-5-sulfony(Dansyl) derivatives of amino acids by reverse-phase high performance liquid chromatography with Nova-Pak C18 column. Determined solvent system was solvent A(200mA phosphate buffer pH 6.8 15%, acetonitrile 11%, water 74%) and solvent B(acetonitrile 65%, methanol 28%, water 7%). Linear gradient of solvent B was applied from 12% to 80% for 50min. Complete separation of 20 amino acids including asparagine and glutamine which constitute protein was achieved within 50min. As the detection limit was the range of picomole, the resolution power was excellent. Reproducibility of the retention time was less than mean $\pm$0.05min. According to the above optimum chromatographic conditions, the amino acid composition of some food and human blood was examined. The most affluent amino acid was alanine in human blood, aspartic acid and glutamic acid in soy sauce, alanine and threonine in soy milk and proline in milk and yoghurt.

• Journal of the Korean Electrochemical Society
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• v.15 no.3
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• pp.190-197
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• 2012

We employed the vinyl ethylene carbonate (VEC) as an electrolyte additive and investigated the effect of the electrolyte additive on the electrochemical performance in hybrid capacitor. The activated carbon was adopted as cathode material, and the $Li_4Ti_5O_{12}$ oxide was used as anode material. The electrolyte was prepared with the $LiPF_6$ salt in the mixed solvent of ethylene carbonate (EC), dimethyl carbonate (DMC), and ethyl methyl carbonate(EMC). We evaluated the electrochemical performance of the hybrid capacitor with increasing the amount of the VEC electrolyte additive, which is known as the remover of oxygen functional group and the stabilizer of the electrode by reducing the surface of electrode, and obtained the superior performance data especially at the addition of the VEC electrolyte additive of around 0.7 vol%. On the contrary, the addition of the VEC more than 0.7 vol% in the electrolyte leads to the degradation in electrochemical performance of hybrid capacitor, suggesting the increase of the side reaction from the excessive VEC additive. X-ray photoelectron spectroscopy (XPS) revealed that the addition of the VEC suppressed the formation of LiF component, which is known as the insulator, on the surface of electrode. The optimized addition of VEC exhibited the improved capacity retention around 82.7% whereas the bare capacitors without VEC additive showed the 43.2% of capacity retention after 2500 cycling test.

• Proceedings of the Ginseng society Conference
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• 1984.09a
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• pp.257-275
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• 1984

Enzymatic browning is considered desirable in tea and tobacco processing but undesirable in many fruits processing at the present time. It is necessary to understand the nature of the enzyme, phenoloxidase, in order to control browning reactions, and extend its effects to formation of browning products as antioxidants in ginseng. Ginseng exhibits antioxidant activity when incorporated with turkey dark meat patties. The activity in red ginseng showed about two times stronger than white ginseng. One of the phenolic antioxidants from fresh, white and reprocessed white ginseng was identified as phenol 2.6 Bis(1.1 dimethyl ethyl) 4-methyl among several unknown compounds by GC/mass spectrometer. In red ginseng, no phenol 2.6 Bis (1.1 dimethyl ethyl) 4-methyl was detected, the compound may be polymerized by phenoloxidase and form some higher molecular compounds which may possess high antioxidant activity. Phenoloxidase isozymes in fresh Korean ginseng (panax ginseng C.A. Meyer) were extracted with phosphate buffer at pH 7.3. The isozymes were purified through ammonium sulfate fractionation, dialysis and chromatography on a DEAE-cellulose column. Two groups of phenoloxidase were shown to be present, one in the floating agglomerated group and the other in the precipitate. group from the 0.85 saturation ammonium sulfate. The DEAE-cellulose column chromatography, the phenoloxidase isozyme present in the precipitate appears as the first peak (I), and that in the agglomerate in the second peak (II). Isozyme I showed higher activity with catechin and catechal, and isozyme II showed higher activity with p-cresol. The isozyme showed two optimum pH activity one at pH 4.5 and the other at 8.5 with catechin as substrate. Korean ginseng phenoloxidase has high heat stability. When heated at $75^{\circ}C$ for 2 hours, its activity remained $90\%\;and\;80\%$ on phenoloxidase I and II respectively. Phenoloxidase I was most active on (+) catechin followed by p-cresal, catechol and epicatechin. Phenoloxidase II was most active on p-cresal followed by (+) catechin, catechol, p-coumanic acid and epicatechin. Sodium bisulfite, sodium cyanide, ascorbic acid glutachion in the oxidized form, sodium diethyl dithiocarbomate and ethylendiamine tetra acetate (EDTA) acted as inhibitors. Red ginseng color development was initiated by phenoloxidase and finished by a followed sun drying process. The antiaging activity of ginseng may be initiated by the antioxidant in the ginseng.

• Journal of fish pathology
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• v.20 no.3
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• pp.307-313
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• 2007

In this study, a QCM biosensor was made to detect Edwardsiella tarda (E. tarda) using a specific antibody. A 9 MHz AT-cut piezoelectric wafer layered with two gold electrodes of 5mm diameter had a reproducibility of 0.1 Hz in frequency response and was used as the transducer of the QCM biosensor. Self assembled layer (SAM) was conformed on a quartz crystal by treating with 3-mer-captopropionic acid (MPA) and activated with N-ethyl-N'-(3-dimethyl-aminopropyl) carbodiimide (EDC) and N-hydroxysuccinimide (NHS). The resulting NHS group was further converted to hydrazide by the reaction with hydrazine. Aldehyde group was introduced into the carbohydrate moiety of anti-E. tarda antibody by the reaction with periodic acid and was used to immobilise the antibody through the reaction with hydrazide group on the electrode surface. A baseline was established in the presence of phosphate-buffered saline (PBS) and a resonant frequency (F1) was measured. Sample was added to the sensor surface and second resonant frequency (F2) was measured after unbound substances were washed out with PBS several times. Finally, the frequency shift (ΔF) representing the mass change was calculated by subtracting F2 from F1. After adding the oxidized anti-E. tarda antibody to the electrode surface containing hydrazide group, frequency shift of 288.811.4 Hz (mean S.E) was observed, thus proving that considerable amount of antibody was immobilized. In the immunoassay test, the frequency shift of 1877.75 Hz, 580.67 Hz, 221.39 Hz, 7.671.83 Hz (mean S.E) were observed at doses of 1000, 500, 100, 50 g of bacterial cells, respectively. It was also demonstrated that the prepared sensor chip was stable enough to withstand repeated surface regeneration with 0.2 M Tris-glycine and 1 % DMSO, pH 2.3 more than ten times.

• Korean Journal of Materials Research
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• v.24 no.6
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• pp.310-318
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• 2014

In this experiment, a highly porous scaffold of biphasic calcium phosphate (BCP) was prepared using the spongereplica method. The BCP scaffold was coated with 58S bioactive glass (BG) and sintered for a second time. The resulting scaffold was coated with gelatin (Gel) and cross-linked with [3-(3-dimethyl aminopropyl) carbodiimide] and N-Hydroxysuccinamide (EDC-NHS). The initial average pore size of the scaffold ranged from 300 to $700{\mu}m$, with more than 85 % porosity. The coating of BG and Gel had a significant effect on the scaffold-pore size, decreasing scaffold porosity while increasing mechanical strength. The material and surface properties were evaluated by means of several experiments involving scanning electron microscopy (SEM), energy-dispersive X-ray (EDX) and X-ray diffraction (XRD). Cytotoxicity was evaluated using MTT assay and confocal imaging of MC3T3-E1 pre-osteoblast cells cultured in vitro. Three types of scaffold (BCP, BCP-BG and BCP-BG-Gel) were implanted in a rat skull for in vivo evaluation. After 8 weeks of implantation, bone regeneration occurred in all three types of sample. Interestingly, regeneration was found to be greater (geometrically and physiologically) for neat BCP scaffolds than for two other kinds of composite scaffolds. However, the other two types of scaffolds were still better than the control (i.e., defect without treatment).