• Journal of Ginseng Research
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• v.39 no.4
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• pp.398-405
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• 2015

Background: Ginseng has been used as a tonic for invigoration of the human body. In a previous report, we identified a novel candidate responsible for the tonic role of ginseng, designated gintonin. Gintonin induces $[Ca^{2+}]_i$ transient in animal cells via lysophosphatidic acid receptor activation. Gintonin-mediated $[Ca^{2+}]_i$ transient is linked to anti-Alzheimer's activity in transgenic Alzheimer's disease animal model. The previous method for gintonin preparation included multiple steps. The aim of this study is to develop a simple method of gintonin fraction with a high yield. Methods: We developed a brief method to obtain gintonin using ethanol and water. We extracted ginseng with fermentation ethanol and fractionated the extract with water to obtain water-soluble and water-insoluble fractions. The water-insoluble precipitate, rather than the water-soluble supernatant, induced a large $[Ca^{2+}]_i$ transient in primary astrocytes. We designated this fraction as gintonin-enriched fraction (GEF). Results: The yield of GEF was approximately 6-fold higher than that obtained in the previous gintonin preparation method. The apparent molecular weight of GEF, determined using sodium dodecyl sulfate-polyacrylamide gel electrophoresis, was equivalent to that obtained in the previous gintonin preparation method. GEF induced $[Ca^{2+}]_i$ transient in cortical astrocytes. The effective dose (ED50) was $0.3{\pm}0.09{\mu}g/mL$. GEF used the same signal transduction pathway as gintonin during $[Ca^{2+}]_i$ transient induction in mouse cortical astrocytes. Conclusion: Because GEF can be prepared through water precipitation of ginseng ethanol extract and is easily reproducible with high yield, it could be commercially utilized for the development of gintoninderived functional health food and natural medicine.

• Korean Journal of Pharmacognosy
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• v.50 no.1
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• pp.37-45
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• 2019

Portulaca oleracea L. (PL) has been used in traditional medicine herb for treatment of various diseases, such as diarrhea, dysentery, and skin inflammation. Previous studies have shown that the PL regulates the inflammation by inhibition of pro-inflammatory cytokines. Although PL might have improvement effects of intestinal function and bioactive effects, there are not enough studies to demonstrate. This study investigated the effects of KDC16-2 on the improvement of intestinal function and anti-inflammatory effects in vivo and in vitro. The improvement effect of intestinal function was measured fecal amount, water content and intestinal transit rate in KDC16-2 treated ICR mice. As results, compared with the control group, the KDC16-2 group showed a significant increase in wet fecal weight, dry fecal weight and fecal water content. The intestinal transit rate of KDC16-2 group was significantly increased. Based on the results, KDC16-2 is considered to have effects on improving intestinal function. The effect of anti-inflammatory demonstrated by using dextran sulfate sodium (DSS)-induced colitis mice. The mice were administered 3% DSS along with KDC16-2 (100, 300 mg/kg) for 14 days. DSS-induced colitis mice were significantly ameliorated in KDC16-2 treated group, including body weight loss, colon length shortening, tight junction protein of colon and histological colon injury. The levels of inflammatory mediators (IgG2a, IgA, C-reactive protein and Myeloperoxidase) and pro-inflammatory cytokines (tumor necrosis factor (TNF)-${\alpha}$, Interleukin (IL)-6) which are involved in inflammatory responses were increased in the DSS-treated group as compared to those in the control group, and the levels were significantly decreased in the KDC16-2 groups. In addition, we investigated the impact of KDC16-2 on lipopolysaccharide (LPS)-induced inflammatory responses in J774A.1 cells. KDC16-2 inhibited production of prostaglandin E2 (PGE2) and reactive oxygen species (ROS). These results suggested that the KDC16-2 could effectively alleviate the dysfunction of intestinal and inflammatory mediators. Thus, these KDC16-2 can be potentially used as health functional food of intestinal.

• Journal of Korean Society of Water and Wastewater
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• v.37 no.6
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• pp.425-435
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• 2023

Organoleptic parameters such as color, odor, and flavor influence consumer perception of drinking water quality. This study aims to evaluate the taste of the selected bottled and tap water samples using an electronic tongue (E-tongue) instead of a sensory test. Bottled and tap water's mineral components are related to the overall preference for water taste. Contrary to the sensory test, the potentiometric E-tongue method presented in this study distinguishes taste by measuring the mineral components in water, and the data obtained can be statistically analyzed. Eleven bottled water products from various brands and one tap water from I city in Korea were evaluated. The E-tongue data were statistically analyzed using multivariate statistical tools such as hierarchical clustering analysis (HCA), principal component analysis (PCA), and partial least squares discriminant analysis (PLS-DA). The results show that the E-tongue method can clearly distinguish taste discrimination in drinking water differing in water quality based on the ion-related water quality parameters. The water quality parameters that affect taste discrimination were found to be total dissolved solids (TDS), sodium (Na+), calcium (Ca²⁺), magnesium (Mg²⁺), sulfate (SO₄^2-), chloride (Cl^-), potassium (K⁺) and pH. The distance calculation of HCA was used to quantify the differences between 12 different types of drinking water. The proposed E-tongue method is a practical tool to quantitatively evaluate the differences between samples in water quality items related to the ionic components. It can be helpful in quality control of drinking water.

• Asian-Australasian Journal of Animal Sciences
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• v.29 no.1
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• pp.126-133
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• 2016

A gene from Actinomyces sp. Korean native goat (KNG) 40 that encodes an endo-${\beta}$-1,4-glucanase, EG1, was cloned and expressed in Escherichia coli (E. coli) $DH5{\alpha}$. Recombinant plasmid DNA from a positive clone with a 3.2 kb insert hydrolyzing carboxyl methyl-cellulose (CMC) was designated as pDS3. The entire nucleotide sequence was determined, and an open-reading frame (ORF) was deduced. The ORF encodes a polypeptide of 684 amino acids. The recombinant EG1 produced in E. coli $DH5{\alpha}$ harboring pDS3 was purified in one step using affinity chromatography on crystalline cellulose and characterized. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis/zymogram analysis of the purified enzyme revealed two protein bands of 57.1 and 54.1 kDa. The amino terminal sequences of these two bands matched those of the deduced ones, starting from residue 166 and 208, respectively. Putative signal sequences, a Shine.Dalgarno-type ribosomal binding site, and promoter sequences related to the consensus sequences were deduced. EG1 has a typical tripartite structure of cellulase, a catalytic domain, a serine-rich linker region, and a cellulose-binding domain. The optimal temperature for the activity of the purified enzyme was $55^{\circ}C$, but it retained over 90% of maximum activity in a broad temperature range ($40^{\circ}C$ to $60^{\circ}C$). The optimal pH for the enzyme activity was 6.0. Kinetic parameters, $K_m$ and $V_{max}$ of rEG1 were 0.39% CMC and 143 U/mg, respectively.

• Fisheries and Aquatic Sciences
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• v.13 no.2
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• pp.102-111
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• 2010

This study was conducted to investigate the optimal conditions of collagen extraction from scales of yellowfin tuna (Thunnus albacares) using surface response methodology. Four independent variables of NaOH concentration and pretreatment fime in alkali pretreatment and enzyme concentration and treatment time in enzyme hydrolysis were used to predict a model equation for the collagen yield. The determinant coefficient ($R^2$) for the equation was 0.906. The values of the independent variables for the maximum yield were 0.32 N NaOH, 16.38 h alkali pretreatment time, 0.18% enzyme concentration, and 31.02 h enzyme treatment time. In the physicochemical properties of tuna scale collagen, sodium dodecyl sulfate-polyacrylamide gel electrophoresis of tuna scale collagen showed the same migration distances as that of calf skin collagen. The amide A, I, II, and III regions of tuna scale collagen in Fourier transform infrared measurements were shown in the peaks of 3,414 $cm^{-1}$, 1,645 $cm^{-1}$, 1,553 $cm^{-1}$, and 1,247 $cm^{-1}$, respectively. The amount of imino acids in tuna scale collagen was 18.97% and the collagen denaturation temperature was $33^{\circ}C$. The collagen solubility as a function of NaCl concentration decreased to 4% NaCl (w/v) and the collagen solubility as a function of pH was high at pH 2-4 and sharply decreased from pH 4 to pH 7. Viscosity of the collagen solution decreased continuously until $30^{\circ}C$ and this decreasing rate slowed in the temperature range of $35-50^{\circ}C$.

• Journal of Korean Society of Environmental Engineers
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• v.27 no.8
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• pp.787-798
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• 2005

The objectives of this study were to assess extraction kinetics of heavy metals with extraction times and to assess extraction efficiencies of heavy metals with concentrations and kinds of washing solutions. Target materials were obtained from disused metal mines. Washing solutions were water, HCl(0.1, 0.3, 1.0 N), EDTA(0.01, 0.05, 0.1 M), and sodium dodecyl sulfate(SDS, 0.1. 0.5, 1.0%). Extraction efficiencies of heavy metals by water and SDS were below 1%, and extraction efficiencies of Zn and Cd were higher than those of Pb and Cu. As results, water and SDS were not effective in extracting heavy metals from mine tailings as washing solution, but extraction efficiencies of Pb and Cu with SDS solution increased as extraction time increased. Extraction kinetics of heavy metals with HCl and EDTA were faster than those with water and SDS. The majority of heavy metals were extracted within 6 hours, and extraction kinetics was almost independent of the solution concentration. Extraction kinetics of heavy metals after 6 hours was slow, but extraction kinetics was dependent on the solution concentration. Also, as concentrations of HCl and EDTA solution were stronger, heavy metals were extracted rapidly and extraction efficiencies were increased. The extraction efficiency was high in order of Cd>Pb>Zn>Cu in using 1.0 N HCl, and Pb>Cd>Zn>Cu in using 0.1 M EDTA. Consequently, extraction effectiveness was highest for Pb in using HCl, and for Pb and Cd in using EDTA with concentration increase. Extraction time of over 6 hours was not effective in extracting heavy metals.

• Journal of Preventive Medicine and Public Health
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• v.17 no.1
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• pp.269-279
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• 1984

The optimum conditions for measuring cadmium content of less than 0.2ppm by flame atomic absorption spectrophotometry were investigated. The cadmium in urine was extracted by APDC-MIBK for the analysis by atomic absorption spectrophotometry after ashing them by a wet method. 1. Optimum conditions by APDC-MIBK and DDTC-MIBK extractions. The acidic aqueous solution was prepared with appropriate amount of 0.IN nitric acid, 5ml of 25% (W/V) sodium potasstum tartarate, 10ml of saturated ammonium sulfate, and 2ml of 2% APDC(or 1 ml of 5% DDTC) chelating agent. The total volume of solution was adjusted to 55 ml and pH to $2{\sim}10$ (or$7{\sim}10$). The aqueous solution was extracted with 10ml MIBK. Concentration of Triton X-100 did not effect the absorbance for APDC-MIBK extraction of cadmium, but absorbance decreased as the concentration increased for DDTC-MIBK extraction. The sensitivity and detection limits for the cadmium determination from APDC-MIBK extraction were 0.0038ppm and 0.0102, 0.0022ppm and 0.0116 for DDTC-MIBK, and 0.0132ppm and 0.0034 for 0.1N nitric acid. APDC-MIBK and DDTC-MIBK extractions were 3 times higher than 0.1N nitric acid for the sensitivity. 2. Excretion of cadmium in 24-hour urine by APDC-MIBK extraction. Determination of cadmium in urine by atomic absorption spectrophotometry of A.A. (Cd=2 mA) mode and B.C. (Cd=4 mA) mode and B.C. (Cd=4mA, $D_2=20mA$) mode showed some difference (p<0.05). The difference of cadmium determination and recovery according to method of standard additions and standard calibration curve method in urine was not significant (p>0.05, $93.48{\pm}11.78%,\;94.83{\pm}22.00%$). Excretion of cadmium in 24-hour urine collection from normal person and variance analysis within measurement variation was not significant (p>0.05), but between interindividual was significant (0.05). Determination of cadmium content by two different methods of flame atomic absorption spectrophotometry and dithizone colorimetry showed that the results from the two methods can be described by a regression line with a good correlation (y=1.0153x-0.2927, x=Cd by D.C., y=Cd by A.A.S., $r=0.8651^*$, p<0.01).

• Toxicological Research
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• v.13 no.1_2
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• pp.117-125
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• 1997

In order to assess the possibility whether CYP2D is involved in caffeine metabolism, we have purified and characterized the rat liver microsomal cytochrome P4502D1 (CYP2D1), equivalent to CYP2D6 in human liver, and have utilized the reconstituted CYP2D1 in the metabolism of 4 primary caffeine (1, 3, 7-trimethylxanthine) metabolites such as paraxanthine (1, 7-dimethylxanthine), 1, 3, 7-trimethylurate, theophylline (1, 3-dimethylxanthine) and theobromine (3, 7-dimethylxanthine). Rat liver CYP 2D1 has been purified to a specific content of 8.98 nmole/mg protein (13.4fold purification, 1.5% yield) using $\omega$-aminooctylagarose, hydroxlapatite, and DE52 columns in a sequential manner. As judged from sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), the purified CYP2D1 was apparently homogeneous. Molecular weight of the purified CYP2D1 was found to be 51, 000 Da. Catalytic activity of the purified and then reconstituted CYP2D1 was confirmed by using bufuralol, a known subsFate of CYP2D1. The reconstituted CYP2D1 was found to produce to 1-hydroxylbufuralol at a rate of 1.43$\pm$0.13 nmol/min/nmol P450. The kinetic analysis of bufuralol hydroxylation indicated that Km and Vmax values were 7.32$\mu M$ and 1.64 nmol/min/nmol P450, respectively. The reconstituted CYP2D1 could catalyze the 7-demethylation of PX to 1-methylxanthine at a rate of 12.5 pmol/min/pmol, and also the 7- and 3- demethylations of 1, 3, 7-trimethylurate to 1, 3-dimethylurate and 1, 7-dimethylurate at 6.5 and 12.8 pmol/min/pmol CYP2D1, respectively. The reconstituted CYP2D1 could also 3-demethylate theophylline to 1-methylxanthine at 5 pmol/min/pmol and hydroxylate the theophylline to 1, 3-dimethylurate at 21.8 pmol/min/pmol CYP2D1. The reconstituted CYP2D1, however, did not metabolize TB at all (detection limits were 0.03 pmol/min/pmol). This study indicated that CYP2D1 is involved in 3-and 7-demethylations of paraxanthine and theophylline and suggested that CYP2D6 (equivalent to CYP2D1 in rat liver) present in human liver may be involved in the secondary metabolism of the primary metabolites of caffeine.

• Journal of Periodontal and Implant Science
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• v.46 no.5
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• pp.320-328
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• 2016

Purpose: Human saliva, as a vital part of the immune defense system, contains a number of distinct proteins and peptides. Recently human common salivary protein 1 (CSP1) has been identified as an abundant salivary protein and may play a role in promoting the binding of cariogenic bacteria to salivary pellicles. However, nothing else is known regarding the role of CSP1 in periodontology. The aim of this study was to quantify and compare CSP1 levels between healthy subjects and periodontal patients. Methods: This controlled clinical study was conducted in periodontally healthy individuals and patients with chronic periodontitis Chonbuk National University Hospital, with Institutional Review Board approval. Whole saliva samples were collected from 36 healthy subjects and 33 chronic periodontitis patients and analyzed. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immune blotting were conducted to ensure that anti-CSP1 monoclonal antibody (mAb) binds to CSP1 in human saliva. A sandwich enzyme-linked immunosorbent assay (ELISA) system was house-fabricated using mAb-hCSP1#14 and mAb-hCSP1#4 as a capture and a detector mAb, respectively. The CSP1 concentrations in saliva from 36 healthy subjects and 33 periodontal patients were quantified using the CSP1 sandwich ELISA system, and the results were analyzed using the Student's t-test. Results: Immunoblot analysis using mAb-hCSP1 as a probe confirmed that CSP1 in human saliva existed as a single band with a molecular weight of approximately 27-kDa. The quantification of CSP1 concentrations by CSP1 ELISA showed that the median values (25th to 75th percentiles) of periodontal patients and healthy subjects were 9,474 ng/mL (range, 8,434.10,139 ng/mL) and 8,598 ng/mL (range, 7,421.9,877 ng/mL), respectively. The Student's t-test indicated the presence of a statistically significant difference between the 2 groups (P=0.024). Conclusions: The presence of a significant difference in CSP1 levels between healthy subjects and periodontal patients suggests that CSP1 may be a potential biomarker for the detection or screening of periodontitis patients.

• Journal of Food Hygiene and Safety
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• v.23 no.4
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• pp.319-323
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• 2008

Analytical method for determination of florfenicol was developed for estimate veterinary drug residue of unestablished MRLs in meat. The method was validated in correspondence with the CODEX guideline for florfenicol residue in meat. The samples mixed with sodium sulfate were extracted with ethyl acetate. After clean-up, the residue was dissolved in mobile phase and analyzed using high-performance liquid chromatography with fluorescence detector. The calibration curve showed good linearity($r^2=0.9997$) within the concentration range of $0.05{\sim}1.0\;mg/kg$. The limit of detection(LOD) and limit of quantification(LOQ) were validated at 0.012 and 0.039 mg/kg, respectively. The recoveries in fortified meat ranged from 85.6 to 95.6%($1.1{\sim}5.3%$ RSD) at the 0.05 to 0.4 spiking levels. We monitored 150 samples of meats that were purchased in Korea(Seoul, Busan, Daegu, Daejeon and Gwangju). Among tested samples, florfenicol was detected in 1 of pig at the level of 0.040 mg/kg, and below LOQ in 1 of cattle, 2 of pig and 2 of chicken. The residues of florfenicol in the tested samples were within the MRLs.