• Korean Journal of Materials Research
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• v.10 no.3
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• pp.233-240
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• 2000

In order to fabricate dense cordierite ceramics without sintering aid, thermal behavior of Mg-Al-Si compounds during sintering was investigated. The dispersibility of cordierite suspension in aqueous media was measured by ESA(electrokinetic sonic amplitude). To prevent aggregation and insufficient dispersion of the cordierite sol, the pH of the suspension was controlled to 1.03 and 8.30 by adding $2N\;HNO_3$ and $2N\;NH_4OH$, respectively. Magnesium-aluminum-silicate complex gel coexisted in the specimen which has been gelled at $150^{\circ}C$ fir 12 hours, however several metastable phase such as ${\mu}-cordierite(Mg_2Al_4Si_5O_{18}),\;spine(MgAl_2O_4)\;and\;mullite(Al_6Si_2O_{13})$ existed below $1300^{\circ}C$ Nucleation rates of the two suspension were similar, but densification of the gel was sensitive to the pH of the sol. Densification of the sol with the pH of 8.3 was more pronounced than that of the sol with pH of 1.63.

• Elastomers and Composites
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• v.44 no.4
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• pp.429-435
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• 2009

The pressure sensitive adhesives (PSA) were synthesized by soap-free emulsion polymerization of acrylic monomers such as butyl acrylate, 2-ethyl hexyl acrylate, and acrylic acid in the presence of starch as a protective colloid and copolymer. The peel strength and holding power of PSA were increased with starch contents due to the enhancement of gel content, But the initial tackiness of PSA was decreased with starch contents. The contact angle analysis of PSA indicated that the wettability was increased with starch contents owing to the increase of polarity by hydroxy group in starch. In the pH measurement of emulsion with time for biodegradability, the starch in the PSA accelerated the lowering of pH due to the formation of organic acids followed by decomposition of starch.

• Molecules and Cells
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• v.39 no.1
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• pp.46-52
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• 2016

It is increasingly apparent that nature evolved peroxiredoxins not only as $H_2O_2$ scavengers but also as highly sensitive $H_2O_2$ sensors and signal transducers. Here we ask whether the $H_2O_2$ sensing role of Prx can be exploited to develop probes that allow to monitor intracellular $H_2O_2$ levels with unprecedented sensitivity. Indeed, simple gel shift assays visualizing the oxidation of endogenous 2-Cys peroxiredoxins have already been used to detect subtle changes in intracellular $H_2O_2$ concentration. The challenge however is to create a genetically encoded probe that offers real-time measurements of $H_2O_2$ levels in intact cells via the Prx oxidation state. We discuss potential design strategies for Prx-based probes based on either the redoxsensitive fluorophore roGFP or the conformation-sensitive fluorophore cpYFP. Furthermore, we outline the structural and chemical complexities which need to be addressed when using Prx as a sensing moiety for $H_2O_2$ probes. We suggest experimental strategies to investigate the influence of these complexities on probe behavior. In doing so, we hope to stimulate the development of Prx-based probes which may spearhead the further study of cellular $H_2O_2$ homeostasis and Prx signaling.

• Journal of agriculture & life science
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• v.43 no.2
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• pp.31-38
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• 2009

The DNA sequencer is known to be more sensitive for the quality of template DNA, method of purification followed by sequencing reaction, and gel concentration. Therefore, we investigated optimal conditions for template preparation, purification, sequencing reaction, gel concentration, and injection medium. For plasmid prepara- tion, using chloroform instead of phenol improved the average read length from 532 bp to 684 bp. The addition of 2.5% DMSO sequencing PCR reaction resulted in 200 bp longer sequences. Purification using 50 mM EDTA and 0.6 M Sodium acetate(pH 8.0) presented 20 bp longer sequences than that using 50 mM EDTA(pH 8.0) and 0.6 M sodium acetate(pH 5.2). The injection for sequencing analysis using ABI formamide presented 90 bp longer sequences than that of using formamide deionized by resin. Moreover, there were 150 bp more readable sequences in 3.6% PAGE gel than in 4%. Consequently, it was concluded that an average of 700 bp per reaction with 85% accuracy can be obtained by the following optimal conditions: template preparation using chloroform, 2.5% DMSO, 50 mM EDTA and 0.6 M sodium acetate(pH 8.0), ABI formamide and 3.6% gel concentration.

• Bulletin of the Korean Chemical Society
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• v.30 no.7
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• pp.1516-1520
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• 2009

A sensitive technique for the determination of trace Co(II) in various samples after column preconcentration by adsorbing onto silica gel loaded with 1-nitroso-2-naphthol was developed. Several experimental conditions, such as pH of sample solution, the amount of silica gel loaded with 1-nitroso-2-naphthol, the flow rate for adsorption and so forth, were optimized. The interfering effects of diverse concomitant ions were investigated. Fe(III) interfered with more than any other ions, but the interference by Fe(III) was completely eliminated by adjusting the amount of silica gel loaded with 1-nitroso-2-naphthol to 0.30 g. The dynamic range, the correlation coefficient ($R^2$), and the detection limit obtained by the proposed technique were 3.0-140.0 ng m$L^{-1}$, 0.9942, and 1.81 ng m$L^{-1}$, respectively. For validating the technique, the aqueous samples (tap water, reservoir water, stream water, and wastewater) and the plastic samples were used as real samples. Recovery yields of 93.0-107.0% were obtained. These measured data were not different from ICP-MS data at the 95% confidence level by F test. Based on the results of the experiment, it has been found that the proposed technique can be applied to the determination of Co(II) in various real samples.

• Journal of Veterinary Clinics
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• v.8 no.1
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• pp.31-45
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• 1991

Present experiment was performed in order to establish the optimal reaction conditions for determination of urinary AAP and GRS activities and to investigate the applicability of urinary AAP and GRS in nephrotoxicity test in rat. The results were as follows ; 1. The optimal pH of phosphate buffer for determination of urinary AAP activity was 7.8. 2. The Michaelis constant of urinary AAP ranged from 0.8 to 1.0mmol/$\ell$ 3. The optimal wave length for determination of urinary GRS activity was 405nm. 4. The optimal pH of acetate buffer for determination of urinary GRS activity was 5.6. 5. The Michaelis constant of urinary GRS ranged from 0.65~0.79mmo1/$\ell$. 6. The AAP activities in gel-filtered samples were significantly higher than those in crude samples. Mean values of AAP activities in gel-filtered samples and crude samples were 29$\pm$20 and 20$\pm$13U/$\ell$, respectively. 7. There was not significant difference between gel-filtered samples and crude samples in urinary GRS activities. Mean values of GRS activities in gel-filtered samples and crude samples were 57$\pm$40 and 56$\pm$39U/$\ell$, respectively. 8. Limits of linearity of urinary AAP and GRS activities were 2.0 and 3.6U/$\ell$, respectively. 9. Within-run imprecisions of the assays, were acceptable, as the coefficients of the AAP activities ranged from 5.5 to 6.3% and those of GRS activities ranged from 1.4 to 6.2%, respectively. 10. Urinary AAP excretion was 675$\pm$227mu/24hrs.kg before administration of potassium dichromate, and increased significantly to 4246$\pm$2567mU/24hrs.kg within 24 hours after administration of potassium dichromate. 11. Urinary GRS excretion did not increase significantly after administration of potassim dichromate. 12. From these findings it is concluded that urinary AAP excretion is early and sensitive Indicator to detect kidney damage in nephrotoxicity experiment.

• Microbiology and Biotechnology Letters
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• v.17 no.1
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• pp.69-73
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• 1989

Cellular autolytic enzyme was isolated from the supernatant fluid of exponentially growing cuiture of Cl. butyricum ID-113. The autolysin was partially pruified by ammonium sulfate fractionation, chromatography on DEAE-Sephadex A-50 and gel filtration through Sephadex G-200. This autolytic enzyme lysed SDS-treated cell wall fractions of Cl. butyricum ID, but not whole cells at all. Its optimum pH and temperature were 5.0 and 37$^{\circ}C$, respectively. This enzyme was relatively stable at neutral pH, but sensitive to heat treatment. Enzyme activity was not influenced by the addition of various divalent cation, but inhibited by Cu$^{++}$.

• Microbiology and Biotechnology Letters
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• v.22 no.6
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• pp.700-706
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• 1994

Lactic acid bacteria in Kimchi fermentation were tested for inhibitory activity against Gram positive bacteria and Gram negative bacteria. The Lactobacillus brevis (KCCM 35464) was found to produce a antimicrobial substance. It showed relatively wide range of inhibition spectrum against gram positive and gram negative bacteria and maintained the inhibitory activity between pH 4.0 and pH 9.0. The antimicrobial substance was obtained in the stationary growth phase and was purified by gel chromatography. The inhibitory effect of the antimicrobial substance on sensitive bacterial strains was determined by filter paper test. The activity of antimicrobial substa- nce was stable at 75$\circ$C. On the basis of its electrophoretic pattern is SDS-PAGE, antimicrobial substance appeared as a single band of 59 KDalton.

• Journal of Microbiology and Biotechnology
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• v.3 no.3
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• pp.188-193
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• 1993

Superoxide dismutase (SOD) was purified from Pseudomonas polycolor to an electrophoretically homogeneous state and partially characterized. SOD was purified by ammonium sulfate fractionation, column chromatography on DEAE-Sephadex A-50, phenyl-Toyopearl 650 M, and gel filtration on Sephadex G-100. The molecular weight and subunit molecular weight of the purified enzyme were estimated to be 40, 000 and 20, 000, respectively. The purified enzyme remained stable at pH 9.0~11.0, $25^{\circ}C$ for 40 hr, but rapidly became inactive below 9.0. SOD was stable up to $45^{\circ}C$ at pH 9.0 with about 80% relative activity, but rapidly became inactive at temperature above that. The enzyme was insensitive to cyanide and fluoride, and sensitive to hydrogen peroxide and azide. The results suggest that the enzyme be an iron-containing SOD.

• Journal of Microbiology
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• v.33 no.3
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• pp.244-251
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• 1995

An extracellular protease of Salmonella schottmulleri was purified from culture filtrate by using 0-75% ammonium sulfate precipitation, DEAE Sepharose Fast Flow ion exchange chromatography, Ultrogel HA chromatography and Sephacryl S-200 HR molecular sieve chromatography. To measure enzyme activity, synthetic dipeptide substrate (CBZ-arg-arg-AFC) with low molecular weight was employed as substrate. The molecular weight of the purified enzyme was approximately 80 kDa when determined by gel filtration on Sephacryl S-200 HR and 73 kDa when estimated by SDS-PAGE. The isoelectric point was 5.45. The activity of the purified enzyme was inhibited by metal chelating agesnts such as EDTA and 1.10-phenanthroline. The divalent cations, such as Ca$\^$2+/, Zn$\^$2+/, Fe$\^$2+/, Mg$\^$2+/ enhanced its activity. These results suggested that it was a metalloprotease. It had a narrow pH optimum of 6.5-7.5 with a maximum at pH 7.0 and a temperature optimum of 40.deg.C. It was stable at least for 1 week at 40.deg.C and maintained its activity for 24 hours at 50.deg.C, but it was rapidly inactivated at 65.deg.C. This protease was shown to be sensitive to sodium 50.deg.C, but it was rapidly inactivated at 65.deg.C. This protease was shown to be sensitive to sodium 50.deg.C, but it was rapidly inactivated at 65.deg.C. This protease was shown to be sensitive to sodium 50.deg.C, but it was rapidly inactivated at 65.deg.C. This protease was shown to be sensitive to sodium dodecyl sulfate (SDS) and was inactivated in a dose-dependent manner. However, it was resistant to Triton X-100 and the activity was enhanced to 32.3% with treatment of 0.025% Triton X-100.