• Korean Journal of Food Science and Technology
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• v.39 no.4
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• pp.438-446
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• 2007

The fermented soybean product, cheonggukjang, is favored by many people, partly due to its bio-functional ingredients. Since the fermentation process of cheonggukjang is mediated by enzymes, including proteases, produced by microbes, analysis of the proteome profile changes in cheonggukjang during fermentation would provide us with valuable information for fermentation optimization, as well as a better understanding of the formation mechanisms of the bio-functional substances. The soluble proteins from cheonggukjang were prepared by a phenol/chloroform extraction method, in order to remove interfering molecules for high resolution 2-D gel analysis. Proteomic analysis of the cheonggukjang different fermentation periods suggested that most of the soluble soy proteins were degraded into smaller forms within 20hr, and many microbial proteins, such as mucilage proteins, dominated the soluble protein fraction. The proteomic profile of cheonggukjang was very different from natto, in terms of the 2-D gel protein profile. Among the separated protein spots on the 2-D gels, 50 proteins from each gel were analyzed by MALDI-TOF MS and PMF for protein identification. Due to database limitations with regard to soy proteins and microbial proteins, identification of the changed proteins during fermentation was restricted to 9 proteins for cheonggukjang and 15 for natto. From de novo sequencing of the proteins by a tandem MS/MS, as well as by database searches using BLASTP, a limited number of proteins were identified with low reliability. However, the 2-D gel analysis of proteins, including protein preparation methods, remains a valuable tool to analyze complex mixtures of proteins entirely. Also, for intensive mass spectrometric analysis, it is also advisable to focus on a few of the interestingly changed proteins in cheonggukjang.

• Korean Journal of Food Science and Technology
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• v.27 no.6
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• pp.1017-1027
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• 1995

This study was attempted to investigate physicochemical properties, molecular structural properties of native and acid-treated chestnut starch and chestnut starch gel. The amylose content was 18.9% and X-ray diffraction pattern showed Cb type. Swelling power was increased abruptly in the range of $65^{\circ}C{\sim}75^{\circ}C$ but increased slowly after that and solubility was increased abruptly until $70^{\circ}C$ but increased slowly after that. In amylograms which have different heating temperatures, cooling viscosity at $50^{\circ}C$ was reduced as heating temperature was increased. In molecular structural properties of amylose, ${\lambda}_{max}$ was 640 nm, ${\beta}-amylolysis$ limit was 84.2% and the degree of polymerization was 951 and in those of amylopectin, ${\lambda}_{max}$ was 570 nm, ${\beta}-amylolysis$ limit was 58.2%, the degree of polymerization was 1371 and average chain length was 22.6. In gel chromatography elution profiles of starch and amylose, 4.0% and 11.5% of low molecular weight-molecules($<5{\times}10^5$) were leached out. In gel chromatography elution profiles of soluble starch, the higher heating temperature was, the more high molecular weight-starches were leached out. The elution profiles after debranching amylopectin with pullulanase showed 2.2 of the ratio of peakIII(DP 10-15) to peakII(DP 35-45). Acid hydrolysis extent of 2.2 N HCI-treated starch at $35^{\circ}C$ for 10 days was 96% and hydrolysis rate showed two step pattern which had border line at 4 days. In elution profiles of acid treated chestnut starch, amylopectin peak was disappeared compeletly after 6 hrs and converted short chains of DP 10-15. Amylose content was increased until 6 hrs but decreased after that. Hardness of starch gel made at $75^{\circ}C$ of heating temperature and cohesiveness of starch gel made at $85^{\circ}C$ of heating temperature were the highest. Retrogradation rate of starch gels were relatively high, especially for the starch gel made at $75^{\circ}C$ of heating temperature.

• Korean Journal of Food Science and Technology
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• v.32 no.3
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• pp.590-597
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• 2000

The rheological properties of ${\beta}-glucans$ isolated from non-waxy and waxy barley were investigated. ${\beta}-Glucan$ solutions showed pseudoplastic properties and their behaviors were explained by applying Power law model in the range of concentrations$(1{\sim}4%)$ and temperatures$(20{\sim}65^{\circ}C)$. The effects of temperature and concentration on the apparent viscosity at $700\;s^{-1}$ shear rate were examined by applying Arrhenius equation and power law equation, and their effect was more pronounced in waxy ${\beta}-glucan$ solutions. The activation energy for flow of ${\beta}-glucan$ solutions decreased with the increase of concentration, and the concentration-dependent constant A increased with the increase of temperature. The intrinsic viscosity of waxy ${\beta}-glucan$ was higher than that of non-waxy ${\beta}-glucan$. The transition from dilute to concentrate region occurred at a critical coil overlap parameter $C^*[{\eta}]=0.02.$ The slopes of non-waxy and waxy ${\beta}-glucan$ at $C[{\eta}] were similar, but the slope of waxy ${\beta}-glucan$ at $C[{\eta}]>C^*[{\eta}]$ was higher than that of non-waxy ${\beta}-glucan$. Dynamic viscoelasticity measurement showed that cross-over happened, and storage modulus was higher than loss modulus at frequency range above cross-over. ${\beta}-Glucan$ solutions formed weak gels after stored for 24 hr.

• Journal of Life Science
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• v.25 no.7
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• pp.826-832
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• 2015

This study describes the effects of activated charcoal on the removal of salts, detergents, and pigments from protein extracts of ginseng leaves and roots. Incubation of protein extracts with 5% (w/v) activated charcoal (100-400 mesh) for 30 min at 4℃ almost removed the salts and detergents including NP-40 as can be observed on SDS-PAGE. In addition, analysis of chlorophyll content showed significant depletion of chlorophyll (~33%) after activated charcoal treatment, suggesting potential effect of activated charcoal on removal of pigments too along with the salts and detergents. 2-DE analysis of activated charcoal treated protein samples showed better resolution of proteins, further indicating the efficacy of activated charcoal in clearing of protein samples. In case of root proteins, although not major differences were observed on SDS-PAGE, 2-DE gels showed better resolution of spots after charcoal treatment. In addition, both Hierarchical clustering (HCL) and Principle component analysis (PCA) clearly separated acetone sample from rest of the samples. Phenol and AC-phenol samples almost overlapped each other suggesting no major differences between these samples. Overall, these results showed that activated charcoal can be used in a simple manner to remove the salts, detergents and pigments from the protein extracts of various plant tissues.

• Journal of the Korean Electrochemical Society
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• v.1 no.1
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• pp.1-7
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• 1998

For the purpose of finding new cathode materials for medium-temperature $(700\~800^{\circ}C)$ solid oxide fuel cells, $Gd_{0.8}Ca_{0.2}Co_{1-x}Fe_xO_3,\;(x=0.0\~0.5)$ are prepared, and their thermal stability and conductivity characteristics are investigated. Also, the cathodic activities are measured after the cathode layer being attached on CGO (cerium-gadolinium oxide) electrolyte disk. The X-ray analyses indicate that the materials prepared by calcining the citrate-gels at $800^{\circ}C$ have the orthorhombic perovskite structure without discernible impurities. The thermal stability of the undoped Co perovskite is so poor that it is decomposed to the individual binary oxide even at $1300^{\circ}C$. But the partially Fe-doped cobaltates exhibit a better thermal stability to retain their structural integrity up to $1400^{\circ}C$. The observation whereby both the undoped and Fe-doped cobaltates melt at ca. $1300^{\circ}C$ leads us to perform the electrode adhesion at <$1300^{\circ}C$. The cathodic activity of $Gd_{0.8}Ca_{0.2}Co_{1-x}Fe_xO_3,\;(x=0.0\~0.5)$, electrodes is superior to $La_{0.9}Sr_{0.1}MnO_3$, among the samples of $x=0.0\~0.5$, the x=0.2 cathode shows the best activity for the oxygen reduction reaction. It is likely that the Fe-doping provides a better thermal stability to the materials but in turn imparts an inferior cathodic activity, such that the optimum trade-off is made at x=0.2 between the two factors. The total electrical conductivity and ion conductivity of $Gd_{0.8}Ca_{0.2}Co_{1-x}Fe_xO_3$, are measured to be 51 S/cm and $6.0\times10^{-4}S/cm\;at\;800^{\circ}C$, respectively. The conductivity values illustrate that the materials are a mixed conductor and the reaction sites can be expanded to the overall electrode surface, thereby providing a better cathodic activity than $La_{0.9}Sr_{0.1}MnO_3$.

• Tuberculosis and Respiratory Diseases
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• v.41 no.3
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• pp.215-221
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• 1994

Background: It is well known that oxygen free radicals(OFR) play a vital role in the various type of acute lung injury. Among various antioxidant defense mechanisms, the superoxide dismutases(SOD) are thought to be the first line of antioxidant defense by catalyzing the dismutation of two superoxide radicals to yield hydrogen peroxide and oxygen. Eukaryotic cells contain two types of intracellular SOD : cytosolic, dimeric copper/zinc- containing enzyme(CuZnSOD) and mitochondrial, tetrameric manganese-containing enzyme(MnSOD). The purpose of this study is to evaluate the time-dependent gene expression of MnSOD and CuZnSOD in the endotoxin-treated rats, and to compare with the manifestations of LPS-induced acute lung injury in rats. Methods: Total RNA from rat lung was isolated using single step phenol extraction 0, 1, 2, 4, 6, 12, 18, 24 hours after E. coli endotoxin injection(n=3, respectively). RNA was separated by formaldehyde-containing 1.2% agarose gels elctrophoresis, transblotted, baked, prehybridized, and hybridized with $^{32}P$-labeled cDNA probes for rat MnSOD and CuZnSOD, which were kindly donated by Dr. Ho(Duke University, Durham, NC, USA). The probes were labeled by nick translation. Blots were washed and autoradiography were quantitated using laser densitometry. Equivalent amounts of total RNA/gel were assessed by monitoring 28S and 18S rRNA. Results: Endotoxin caused a rise in steady-state MnSOD mRNA levels by 4h with peak mRNA accumulation by 6h. Continued MnSOD mRNA expression was observed at 12h. CuZnSOD mRNA expression was observed from 1h to 24h with peak levels by 18h. Conclusion: These results suggest that SOD palys an important defensive role in the endotoxin-induced acute lung injury in rats.

• Bulletin of the Korean Chemical Society
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• v.30 no.6
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• pp.1285-1292
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• 2009

Large single crystals of zeolite, |$Na_{75}$|[$Si_{117}Al_{75}O_{384}$]-FAU (Na-Y, Si/Al = 1.56), were synthesized from gels with composition of 3.58Si$O_2$ : 2.08NaAl$O_2$ : 7.59NaOH : 455$H_2$O : 5.06TEA : 2.23TCl. One of these, a colorless single-crystal was ion exchanged by allowing aqueous 0.02 M CsOH to flow past the crystal at 293 K for 3 days, followed by dehydration at 673 K and 1 ${\times}\;10^{-6}$ Torr for 2 days. The crystal structure of fully dehydrated partially $Cs^+$-exchanged zeolite Y, |$Cs_{45}Na_{30}$|[$Si_{117}Al_{75}O_{384}$]-FAU per unit cell (a = 24.9080(10) $\AA$) was determined by single-crystal X-ray diffraction technique in the cubic space group Fd $\overline{3}$ m at 294(1) K. The structure was refined using all intensities to the final error indices (using only the 877 reflections with $F_o\;>\;4{\sigma}(F_o))\;R_1$ = 0.0966 (Based on F) and $R_2\;=\;0.2641\;(Based\;on\;F^2$). About forty-five $Cs^+$ ions per unit cell are found at six different crystallographic sites. The 2 $Cs^+$ ions occupied at site I, at the centers of double 6-ring (D6Rs, Cs-O = 2.774(10) $\AA$ and O-Cs-O = 88.9(3) and 91.1(3)$^o$). Two $Cs^+$ ions are found at site I’ in the sodalite cavity; the $Cs^+$ ions were recessed 2.05 $\AA$ into the sodalite cavity from their 3-oxygen plane (Cs-O = 3.05(3) $\AA$ and O-Cs-O = 77.4(13)$^o$). Site-II’ positions (opposite single 6-rings in the sodalite cage) are occupied by 7 $Cs^+$ ions, each of which extends 2.04 $\AA$ into the sodalite cage from its 3-oxygen plane (Cs-O = 3.067(11) $\AA$ and O-Cs-O = 80.1(3)$^o$). The 26 $Cs^+$ ions are nearly three-quarters filled at site II in the supercage, being recessed 2.34 $\AA$ into the supercage (Cs-O = 3.273(8) $\AA$ and O-Cs-O = 74.3(3)$^o$). The 4 $Cs^+$ ions are found at site III deep in the supercage (Cs-O = 3.321(19) and 3.08(3) $\AA$), and 4 $Cs^+$ ions at another site III’ (Cs-O = 2.87(4) and 3.38(4) $\AA$). About 30 $Na^+$ ions per unit cell are found at one crystallographic site; The $Na^+$ ions are located at site I’ in the sodalite cavity opposite double 6-rings (Na-O = 2.578(11) $\AA$ and O-Na-O = 97.8(4)$^o$).

• Tuberculosis and Respiratory Diseases
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• v.45 no.5
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• pp.984-991
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• 1998

Background: The 3p deletions has been shown to be the most frequent alteration in lung cancers, strongly suggesting the presence of at least one tumor suppressor gene in this chromosomal region. However, no solid candidate for the tumor suppressor gene(s) on 3p has as yet been identified. Recent attention has focused on a candidate 3p14.2 tumor suppressor gene, FHIT, which is located in a region that is homozygously deleted in multiple tumor cell lines and disrupted by the hereditary renal cell carcinoma t(3;8) chromosomal translocation breakpoint FHIT also spans FRA3B, the most common fragile sites in the human genome. In the present study, we have analyzed expression of the FHIT gene in lung cancer cell lines. Methods: RNA from 21 lung cancer cell lines (16 NSCLC, 5 SCLC) were extracted using standard procedures. Random-primed. first strand cDNAs were synthesized from total RNA and PCR amplication of coding exons 5 to 9 was performed. The RT-PCR products were electrophoresed in 1.5% ethidium bromide-stained agarose gels. Results: 12 of 21(57%) lung cancer cell lines exhibited absent or aberrant FHIT expression [7 of 16(44%) of non-small cell lung cancer and 5 of 5(100%) of small cell lung cancer cell lines]. Conclusion: The result shows that abnormal transcription of the FHIT gene is common in human lung cancer cell lines, especially in small cell lung cancer.

• Restorative Dentistry and Endodontics
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• v.23 no.1
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• pp.141-161
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• 1998

The depth and patterns of demineralization according to the difference in concentration and application time of phosphoric acid were observed through the transmission electron microscope, and shear bond strengths to the acid -conditioned dentin were then measured and compared with the TEM results. To investigate the influence of polymer addition into the phosphoric acid and the effect of difference in concentration and application time of the acid, the specimens were randomly divided into 9 groups. Among the specimens, the exposed dentin surfaces were acid-conditioned with 10% polymer-thickened phosphoric acid(All Bond 2, Bisco, U.S.A.) and aqueous 10%, 20%, 30%, 40% phosphoric acid for 20 seconds, The rest of the specimens were acid-conditioned with 10% phosphoric acid for 15s, 30s, 60s, 120s respectively. The specimens were immersed in 4% glutaraldehyde in 0.1M sodium cacodylate buffer and postfixed with 1 % osmium tetroxide without decalcification and then observed under a JEOL Transmission Electron Microscope(JEM 1200 EX II, Japan). After the specimens were acid-conditioned as the above, primer and adhesive resin were applied to blot-dried dentin and shear bond strengths were then measured and analysed. The results were as follows : 1. The intertubular demineralization depth of 4.0-$5.0{\mu}m$ in 10% polymer-thickened phosphoric acid gels was similar or slightly deeper than that of 4.0-$4.5{\mu}m$ in aqueous 10% phosphoric acid solution. 2. The intertubular demineralization depth of aqueous 20%, 30% and 40% phosphoric acid solution was 6.5-$7.0{\mu}m$, 6.5-$7.5{\mu}m$ and 9.0-$15.0{\mu}m$ respectively. It showed that the depth of dentin demineralization is partly related to the concentration of phosphoric acid solution. 3. The intertubular demineralization depth of aqueous 10% phosphoric acid solution in application time for 15s, 30s, 60s and 120s was 2.5-$3.0{\mu}m$, 4.0-$6.0{\mu}m$, 6.5-$7.0{\mu}m$ and 8.5-$14.0{\mu}m$ respectively. It showed that the depth of dentin demineralization is directly related to the application time of phosphoric acid solution. 4. The partially demineralized dentin layer between demineralized collagen layer and unaffected dentin was showed to a width of 0.5-$1.0{\mu}m$ in lower concentration groups treated with aqueous 10% phosphoric acid for 20s, 60s, 120s and 20% phosphoric acid for 20s. 5. The demineralization effect at the border of intertubular-peritubular junction was less evident than that in the peritubular and intertubular dentin. The collagen fibers in the intertubular dentin had a random orientation, whereas those that lined the tubules were circumferentially aligned. The cross-linkage of dentinal collagen in demineralized collagen layer was clearly seen. 6. A statistically significant difference of bond strengths according to the difference in phosphoric acid concentration did not exist among the groups treated with 10%, 20%, 30% and 40% acid solution (P>0.05). However, bond strengths to the treated dentin with 10% phosphoric acid solution for 30s were significantly higher than that for 120s (P<0.05).