• Proceedings of the Korean Geotechical Society Conference
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• 2000.11a
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• pp.615-620
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• 2000

The strength properties of Light-Weighted Soils(LWS) mixed with Expanded Polystrene(E.P.S) are studied. Test results show that when the initial water contents of dredged soils are under 135% and the cement contents are above 1%, Light-Weight Soils are in the appropriate strength range of 2.0 to 4.0kg/㎠. However, E.P.S contents had a little affects on the strength properties of LWS. In the view of E.P.S diagram's effects on LWS, which have expand ratio of 25, 35, 45 and 60, further studies considering of physical properties of original E.P.S beads are needed.

• Applied Biological Chemistry
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• v.26 no.4
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• pp.217-221
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• 1983

$\beta$-Galactosidase($\beta$-D-galactoside galactohydrolase, E.C. 3. 2. 1. 23) from E. coli K-12 CSH 36 was immobilized on porous cellulose beads which were previously activated with tannin and p-benzoquinone. Their general properties and applicational possibities were investigated. The most effective, enzyme immobilization was obtained when tannin and p-benzoquinone, pH 11.0, were used together as activation reagents and a period of 6 hours of activation. The optimum pH of $\beta$-galactosidase was 5.5 for free enzyme and 6. 0 for the immobilized enzyme, the optimum temperatures for native and immobilized enzyme were both $50^{\circ}C$. Kms of native $\beta$-galactosidase and immobilized enzyme for ONPG(o-nitrophenyl galactopyranoside) were about $4.0{\times}10^(-4)M$ and $7.5{\times}10^(-4)M$, respectively. In the case of tannin : p-benzoquinone activated cellulose beads, the immobilized enzyme retained over 80% of the initial enzyme activity after 20 runs, which is very promising result far a possible industrial application.

• Journal of the korean academy of Pediatric Dentistry
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• v.26 no.4
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• pp.652-663
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• 1999

Craniosynostosis, the premature fusion of cranial sutures, presumably involves disturbance of the interactions between different tissues within the cranial sutures. Interestingly, point mutaions in the genes encoding for the fibroblast growth factor receptors(FGFRs), especially FGFR2, cause various types of human craniosynostosis syndromes. To elucidate the function of these genes in the early morphogenesis of mouse cranial sutures, we first analyzed by in situ hybridization the expression of FGFR2(BEK) and osteopontin, an early marker of osteogenic differentiation, in the sagittal suture of calvaria during embryonic(E15-E18) and postnatal stage(P1-P3). FGFR2(BEK) was intensely expressed in the osteogenic fronts, whose cells undergo differentiation into osteoprogenitor cells that ultimately lay down the bone matrix. Osteopontin was expressed throughout the parietal bones excluding the osteogenic fronts, the periphery of the parietal bones. To further examine the role of FGF-mediated FGFR signaling in cranial suture, we did in vitro experiments in E15.5 mouse calvarial explants. Interestingly, implantation of FGF2 soaked beads onto both the osteogenic fronts and mid-mesenchyme of sagittal suture after 36 hours organ culture resulted in the increase of the tissue thickness and cell number around FGF2 beads, moreover FGF4-soaked beads implanted onto the osteogenic fronts stimulated suture closure due to an accelerated bone growth, compared to FGF4 beads placed onto mid-mesenchyme of sagittal suture and BSA control beads. In addition FGF2 induced the ectopic expression of osteopontin and Msx1 genes. Taken together, these data indicate that FGF-mediated FGFR signaling has a important role in regulating the cranial bone growth and maintenance of cranial suture, and suggest that FGF-mediated FGFR signaling is involved in regulating the balance between the cell proliferation and differentiation through inducing the expression of osteopontin and Msx1 genes.

• Journal of Life Science
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• v.25 no.10
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• pp.1164-1168
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• 2015

Previous research showed that chlorphenesin galactoside (CPN-Gal), a preservative in cosmetics, was safer than CPN against human skin cells [9]. To establish a stable and long-term process for CPN-Gal production, we investigated the repeated-batch process. In this process, β-gal-producing recombinant Escherichia coli cells were immobilized in calcium alginate beads, and CPN was converted to CPN-Gal by the transgalactosylation reaction. The process was conducted in a 300 ml flask, which contained E. coli cell-immobilized alginate beads, 33.8 mM of CPN, and 400 g/l of lactose. The pH and temperature were 7.0 and 40℃, respectively. During the repeated-batch operation, four consecutive batch operations were conducted successfully until 192 hr. The conversion yield of CPN to CPN-Gal was 64% during 192 hr, which was higher than the values in previous reports [3, 13]. Thereafter, however, the conversion yield gradually decreased until the operation was finished at 336 hr. Western blotting of immobilized E. coli cells revealed that β-gal gradually decreased after 192 hr. In addition, alginate beads were cracked when the operation was finished. It is probable that, including this loss of E. coli cells by cracks, deactivation, and product inhibition of E. coli β-gal might lead to a gradual decrease in the production of CPN-Gal after 192 hr. However, as the purification of β-gal is not necessary with β-gal-producing recombinant E. coli cells, β-gal-producing E. coli cells might be a practical and cost-effective approach for enzymatically synthesizing CPN-Gal. It is expected that this process will be extended to long-term production process of CPN-Gal for commercialization.

• Journal of the Korean Wood Science and Technology
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• v.29 no.3
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• pp.112-122
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• 2001

Laccase enzymes from Cerrena unicolor and Trametes versicolor were immobilized on the activated glass beads (CPG), silica gel (SG) and soil (SL). The heterogeneous matrices were activated by ${\gamma}$-aminopropyltriethoxysilane (APTES) and glutaraldehyde (GA), and their surfaces were coated by keratin (KER) on activated or non-activated CPG, SG and SL. The laccase activities were tested in the aqueous solution for the native and immobilized preparations using different pH and temperature conditions. By keratin coating on supports, in the cases of CPG-KER and SL-KER, the immobilization yield was increased from about 80% to 90%. Moreover, much less protein was immobilized in keratin coated matrices than in inorganic ones alone (e.g. on CPG-KER 57.6%, whereas on CPG alone 80.6%). Laccase immobilization on keratin coated inorganic matrices was generally more effective than that of non-coated matrices. Concerned to pH dependency, the optima pH for immobilized laccases generally shifted towards to higher values, 5.5-5.8 and even 5.9 in the case of keratin for C. unicolor and from 5.3 to 5.7 for T. versicolor, respectively, and decreased less gradually both in acidic and alkaline regions. The immobilized laccase was more stable against thermal denaturation. This seems particularly true at $75^{\circ}C$ in the case of C. unicolor, where the activity of immobilized enzyme is > 50% higher than that of the free enzyme. For T. versicolor the respective values were $65^{\circ}C$, and 50%.

• The Korea Journal of Herbology
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• v.21 no.2
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• pp.9-13
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• 2006

Objectives : To determine the DNA sequence of the 18S rRNA gene of the Rehmannia glutinosa and analyze it phylogenetically Methods : Dried root of the Rehmannia glutinosa was ground with a mortar and pestle. Glass beads(0.5 mm in diameter), TE buffer and SDS solution were added to that. The mixture was vortexed vigorously and extracted with the mixture of phenol, chloroform and isoamyl alcohol and with the mixture of the chloroform and isoamyl alcohol. The nucleic acids were precipitated with ethanol and resuspended in TE buffer. Contaminating RNA was digested with RNAse A and the DNA was purified further with the Geneclean Turbo Kit. This DNA was used as a template for amplification of the 18S rRNA gene by PCR. The PCR product was cloned in the pBluescript SK II plasmid by blunt-end ligation and the DNA sequence of the insert was determined. This DNA sequence was analyzed phylogenetically by the BLAST program. Results and Conclusion : Vortexing the ground powder of the dried plant root with glass beads during cell lysis improved recovery of DNA. The DNA sequence of the Rehmannia glutinosa 18S rRNA gene was determined and deposited at the GenBank as the accession number DQ469606. Phylogenetic analysis of that sequence showed the relationship between the members of the family of Scrophulariaceae and also the close relationship of the Buddleja davidii to the members of the Scrophulariaceae family.

• Korean Journal of Microbiology
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• v.31 no.4
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• pp.279-285
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• 1993

Alterations of the p53 gene arc among the most frequent genetic changes in human cancer and often result in increased levels of p53 protein within the malignant cells. Detection of accumulated p53 protein can be a useful prognostic tool in human cancer. In order to make polyclonal antibodies for immunohistochemical screening. human p53 gene was expressed in E. coli in the form of GST (glutathione S-transfi.:rase) fusion proteins. Two p53 gene fragments. which were N('()I small fragment encoding amino acid residues of 1-151-: and Ncol large fragment of 159-393. were subeloned into the unique BamHI site present within the pGEX-2T vector using BamHI linker and recombinant plasmids pGTNS and pGTNL were constructed. respectively. The p53 cDNA fragment (from pC53-$SN_3$,) encoding amino acid 38-145 (proline at residue 72) was amplified by polymerase chain reaction(PCR). The amplified DNA was digested with BamHI and Prull and inserted into the BamHI-Smal sites of pG EX-2T and recombinant plasmid pGTBP was constructed. After IPTG induction of these plasmids for 4 hours. fusion proteins were purified from E. coli extracts with glutathione Sepharose beads. The bound proteins were resolved by 10% SDS-polyacrylamide gel electrophoresis and the molecular weights were 54 kDa. 53 kDa and 40 kDa. respectively. Approximately one milligram of fusion proteins were purified from 1 -liter cultures.

• KSBB Journal
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• v.24 no.5
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• pp.432-438
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• 2009

Here, we demonstrated simple nucleic acid, RNA, concentration method using polymer micro chip containing glass bead ($100\;{\mu}m$). Polymer micro chip was fabricated by PDMS ($1.5\;cm\;{\times}\;1.5\;cm$, $100\;{\mu}m$ in the height) including pillar structure ($160\;{\mu}m\;(I)\;{\times}\;80\;{\mu}m\;(w)\;{\times}\;100\;{\mu}m\;(h)$, gap size $50\;{\mu}m$) for blocking micro bead. RNA could be adsorbed on micro glass bead at low pH by hydrogen bonding whereas RNA was released at high pH by electrostatic force between silica surface and RNA. Amount of glass beads and flow rate were optimized in aspects of adsorption and desorption of RNA. Adsorption and desorption rate was measured with real time PCR. This concentrated RNA was applied to amplification micro chip in which NASBA (Nucleic Acid Sequence Based Amplification) was performed. As a result, E.coli O157 : H7 in the concentration of 10 c.f.u./10 mL was successfully detected by these serial processes (concentration and amplification) with polymer micro chips. It implies this simple concentration method using polymer micro chip can be directly applied to ultra sensitive method to measure viable bacteria and virus in clinical samples as well as environmental samples.

• Asian Journal of Atmospheric Environment
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• v.11 no.1
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• pp.15-28
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• 2017

The adsorptive removal properties of synthetic A4 zeolite were investigated against a total of 16 offensive odors consisting of reduced sulfur compounds (RSCs), nitrogenous compounds (NCs), volatile fatty acids (VFAs), and phenols/indoles (PnI). Removal of these odors was measured using a laboratory-scale impinger-based adsorption setup containing 25 g of the zeolite bed (flow rate of $100mL\;min^{-1}$). The high est and lowest breakthrough (%) values were shown for PnIs and RSCs, respectively, and the maximum and minimum adsorption capacity (${\mu}g\;g^{-1}$) of the zeolite was observed for the RSCs (range of 0.77-3.4) and PnIs (0.06-0.104), respectively. As a result of sorptive removal by zeolite, a reduction in odor strength, measured as odor intensity (OI), was recorded from the minimum of approximately 0.7 OI units (indole [from 2.4 to 1.6]), skatole [2.2 to 1.4], and p-cresol [5.1 to 4.4]) to the maximum of approximately 4 OI units (methanethiol [11.4 to 7.5], n-valeric acid [10.4 to 6.5], i-butyric acid [7.9 to 4.4], and propionic acid [7.2 to 3.7]). Likewise, when removal was examined in terms of odor activity value (OAV), the extent of reduction was significant (i.e., 1000-fold) in the increasing order of amy acetate, i-butyric acid, phenol, propionic acid, and ammonia.