• 대한환경공학회지
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• 제22권2호
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• pp.375-383
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• 2000

유일로 오염된 지역의 토양에서 toluene을 탄소원으로 이용하는 혼합미생물을 분리하여 toluene, benzene, ethylbenzene 및 xylene isomers(BTEX)의 분해특성을 관찰하였다. 단일기질 실험에서는 모든 BTEX의 분해가 이루어졌으며 toluene, benzene, ethylbenzene, p-xylene 순서로 분해되었다. BTEX 혼합기질 분해실험에서는 단일기질일 때보다 분해속도가 상대적으로 느려졌으며, ethylbenzene이 benzene보다 먼저 분해되는 것이 관찰되었다. 이중 혼합물질 반응 실험에서는 방해작용(inhibition), 촉진작용(stimulation), 그리고 비반응(non-interaction)과 같은 다양한 기질반응이 관찰되었으며, ethylbenzene은 benzene, toluene, xylene의 분해에 강한 방해영향을 주었다. Xylene 분해특성에서 m- 및 p-xylene은 혼합미생물에 탄소원으로 이용되었으며 benzene이나 toluene이 동시에 존재할 때는 xylene isomer의 분해가 촉진되었다. 그러나 o-xylene의 분해는 benzene에 의해서만 촉진되었다.

• Journal of Microbiology and Biotechnology
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• 제12권6호
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• pp.909-915
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• 2002

The biodegradation of BTEX components (benzene, toluene, ethylbenzene, o-xylene, m-xylene, and p-xylene) individually and in mixtures was investigated using the o-xylene-degrading thermo-tolerant bacterium Ralsronia sp. strain PHS1 , which utilizes benzene, toluene, ethylbenzene, or o-xylene as its sole carbon source. The results showed that as a single substrate for growth, benzene was superior to both toluene and ethylbenzene. While growth inhibition was severe at higher o-xylene concentrations, no inhibition was observed (up to 100 mg $l^-1$) with ethylbenzene. In mixtures of BTEX compounds, the PHS1 culture was shown to degrade all six BTEX components and the degradation rates were in the order of benzene, toluene, o-xylene, ethylbenzene, and m- and p-xylene. m-Xylene and p-xylene were found to be co-metabolized by this microorganism in the presence of the growth-supporting BTEX compounds. In binary mixtures containing the growth substrates (benzene, toluene, ethylbenzene. and o-xylene), PHS1 degraded each BTEX compound faster when it was alone than when it was a component of a BTEX mixture, although the degree of inhibition varied according to the substrates in the mixtures. p-Xylene was shown to be the most potent inhibitor of BTEX biodegradation in binary mixtures. On the other hand, the degradation rates of the non-growth substrates (m-xylene and p-xylene) were significantly enhanced by the addition of growth substrates. The substrate utilization patterns between PHS1 and other microorganisms were also examined.

• Corrosion Science and Technology
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• 제6권4호
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• pp.154-158
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• 2007

For the application of flexible printed circuit board (FPCB), electroplated copper is required to have low surface roughness and residual stress. In the paper, the effects of surface roughness and residual stress of electroplated copper as thick as $8{\mu}m$ were studied on organic additives such as inhibitor, leveler and accelerator. Polyimide film coated with sputtered copper was used as a substrate. Surface roughness and surface morphology were measured by 3D-laser surface analysis and FESEM, respectively. Residual stress was calculated by Stoney's equation after measuring radius curvature of specimen. The addition of additives except high concentration of accelerator in the electrolyte decreased surface roughness of electroplated copper film. Such a tendency was explained by the function of additives among which the inhibitor and the leveler inhibit electroplating on a whole surface and prolusions, respectively. The accelerator plays a role in accelerating the electroplating in valley parts. The inhibitors and the leveler increased residual stress, whereas the accelerator decreased it. It was thought to be related with entrapped additives on electroplated copper film rather than the preferred orientation of electroplated copper film. The reason why additives lead to residual stress remains for the future work.

• 대한본초학회지
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• 제31권1호
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• pp.1-5
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• 2016

Objectives : The purpose of this study was to investigate inhibitory effects of steamed Polygonatum odoratum extract (POE) on insulin resistance in rat skeletal muscle cells, L6 cells.Methods : Polygonatum odoratum (P. odoratum) extract was extracted with ethyl acetate. Activity of α-glucosidase in POE was measured for blood glucose regulation. MTT assay was examined for cell toxicity. Western blot analysis for measurement of adiponectine, peroxisome proliferator-activated receptorγ (PPARγ), insulin receptor substrate (IRS), glucose transporter 4 (Glut-4) and phosphorylation of serine/threonine-specific protein kinase (Akt) expressions were performed. Akt signaling pathway were analyzed with LY294002, which is a specific PI3K/Akt inhibitor.Results : The results revealed that POE inhibited α-glucosidase activity. Treatment of POE in L6 cells inhibited the differentiation of L6 cells compared to those of vehicl control. Additionally, protein expressions of adiponectine, PPARγ, IRS and Glut-4 were significantly regulated compared to those of vehicle control (p < 0.05), respectively. Futhermore, phosphorylation of Akt was increased in L6 cells treated with POE compared to that of vehicle control (p < 0.05). pAkt expression was significantly accentuated with Akt inhibitor (LY294002).Conclusions : These results suggest that POE may have potential as a natural agent for prevention/improvement of diabetes, especially, regulation of blood glucose. Therefore, further additional study should be conducted to elucidate in depth the pharmaceutical efficacy of these.

• Journal of Microbiology
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• 제43권3호
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• pp.237-243
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• 2005

The protease purified from Bacillus cereus JH108 has the function of leucine specific endopeptidase. When measured by hydrolysis of synthetic substrate (N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide), the enzyme activity exhibited optimal activity at pH 9.0, $60^{\circ}C$. The endopeptidase activity was stimulated by $Ca^{++},\;Co^{++},\;Mn^{++},\;Mg^{++},\;and\;Ni^{++}$, and was inhibited by metal chelating agents such as EDTA, 1,10-phenanthroline, and EGTA. Addition of serine protease inhibitor, PMSF, resulted in the elimination of the activity. The endopeptidase activity was fully recovered from the inhibition of EDTA by the addition of 1 mM $Ca^{++}$, and was partially restored by $Co^{++}\;and\;Mn^{++}$, indicating that the enzyme was stabilized and activated by divalent cations and has a serine residue at the active site. Addition of $Ca^{++}$ increased the pH and heat stability of endopeptidase activity. These results show that endopeptidase requires calcium ions for activity and/or stability. A Lineweaver-Burk plot analysis indicated that the $K_m$ value of endopeptidase is 0.315 mM and $V_{max}$ is 0.222 ) is $0.222\;{\mu}mol$ of N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide per min. Bestatin was shown to act as a competitive inhibitor to the endopeptidase activity.

• Fisheries and Aquatic Sciences
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• 제1권2호
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• pp.209-215
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• 1998

Trypsin-like enzyme was purified from shrimp hepatopancreas through Q-Sepharose ionic exchange, benzamidine Sepharose-6B affinity, and Superdex 75 gel chromatography. Purity of trypsin-like enzyme was increased 69-fold with $44\%$ yield. The enzyme consisted of a single polypeptide chain with a molecular weight (M.W.) of 32 kDa judged by sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme was completely inactivated by serine enzyme inhibitors such as soybean trypsin inhibitor (SBTI), tosyl-L­lysine chloromethyl ketone (TLCK), and leupeptin. However, the enzyme was not affected by tosyl-L-phenylalanine chloromethyl ketone (TPCK) which is a chymotrypsin specific inhibitor. The enzyme had no activity against benzoyl-tyrosine ethyl ester (BTEE) which is a chymotrypsin specific substrate. The enzyme showed high activity on the carboxyl terminal of Phe, Tyr. Glu, Arg, and Asp. However. no activity was detected against the carboxyl terminal of Pro, Trp, Cys, Gly, Val, and Ala.

• Bulletin of the Korean Chemical Society
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• 제32권10호
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• pp.3666-3674
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• 2011

Overexpression of P-glycoprotein (Pgp) is associated with multidrug resistance (MDR) of tumor cells to a number of chemotherapeutic drugs. Pgp inhibitors have been shown to effectively reverse Pgp-mediated MDR. We prepared a series of phenoxy-N-phenylacetamide derivatives and tested for their ability to inhibit Pgp as potential MDR reversing agents, using a Pgp over-expressing MCF-7/ADR cell line. Some of the synthesized compounds exhibited moderate to potent reversal activity. Of note, compound 4o showed a 3.0-fold increased inhibition compared with verapamil, a well-known Pgp inhibitor. In addition, co-treatment of the representative compound 4o and a substrate anticancer agent doxorubicin resulted in a remarkable increase in doxorubicin's antitumor effect and inhibition of DNA synthesis in the MCF-7/ADR cell line. Taken together, these findings suggest that compound 4o could be a useful lead for development of a novel Pgp inhibitor for treatment of MDR.

• Corrosion Science and Technology
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• 제19권1호
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• pp.8-15
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• 2020

In this paper, the efficiency and the inhibition mechanisms of cobalt salts (cobalt nitrate and cobalt-exchange silica Co/Si) for the corrosion protection of AA2024 were investigated in a neutral aqueous solution by using the electrochemical impedance spectroscopy (EIS) and polarization curves. The experimental measurements suggest that cobalt cation plays a role as a cathodic inhibitor. The efficiency of cobalt cation was important at the concentration range from 0.001 to 0.01 M. The formation of precipitates of oxides/hydroxides of cobalt on the surface at low inhibitor concentration was confirmed by the Scanning Electron Microscopy/Energy Dispersive X-Ray Spectroscopy (SEM/EDS) analysis. EIS measurements were also conducted for the AA2024 surface covered by water-based epoxy coating comprising Co/Si salt. The results obtained from exposure in the electrolyte demonstrated the improvement of the barrier and inhibition properties of the coating exposed in the electrolyte solution for a lengthy time. The SEM/EDS analysis in artificial scribes of the coating after salt spray testing revealed the release of cobalt cations in the coating defect to induce the barrier layer on the exposed AA2024 substrate.

• BMB Reports
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• 제38권3호
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• pp.343-349
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• 2005

Gamma-glutamyltransferase (GGT, EC 2.3.2.2) which hydrolyzes glutathione (GSH), is required for the maintenance of normal intracellular GSH concentration. GGT is a membrane enzyme present in leukocytes and platelets. Its activity has also been observed in human neutrophils. In this study, GGT was purified from Triton X-100 solubilized neutrophils and its kinetic parameters were determined. For kinetic analyses of transpeptidation reaction, $\gamma$-glutamyl p-nitroanilide was used as the substrate and glycylglycine as the acceptor. Apparent $K_m$ values were determined as 1.8 mM for $\gamma$-glutamyl p-nitroanilide and 16.9 mM for glycylglycine. The optimum pH of GGT activity was 8.2 and the optimum temperature was $37^{\circ}C$. It had thermal stability with 58% relative activity at $56^{\circ}C$ for 30 min incubation. L-serine, in the presence of borate, was detected as the competetive inhibitor. Bromcresol green inhibited neutrophil GGT activity as a noncompetetive inhibitor. The neutrophils seem to contain only the isoenzyme that is present in platelets. We characterized the kinetic properties and compared the type of the isoenzyme of neutrophil GGT with platelet GGT via polyacrylamide gel electrophoresis (PAGE) under a standart set of conditions.

• BMB Reports
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• 제28권6호
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• pp.471-476
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• 1995

Acetolactate synthase (ALS) catalyzes the first common step in the biosynthesis of valine, leucine, and isoleucine. ALS is the target enzyme for several classes of structually diverse herbicides. We have synthesized 4,6-dimethoxypyrimidine derivatives as ALS inhibitors, and their inhibitory activities on barley ALS were determined. $IC_{50}$ values for the derivatives are 0.2~200 ${\mu}m$. K11570, the most potent ALS inhibitor with $IC_{50}$ of 0.2 ${\mu}m$, showed mixed-type inhibition with respect to substrate pyruvate, and the progress curves for ALS inhibition by K11570 indicated that the amount of inhibition increased with time. Inhibition-competition experiments were carried out and indicated that three different classes of inhibitors, K11570, a sulfonylurea Ally, and leucine, bind to ALS in a mutually exclusive manner. Chemical modification of tryptophanyl and tyrosyl residues of ALS decreased the sensitivity of ALS to K11570, while cysteine modification did not affect the sensitivity. These results suggest that tryptophanyl and tyrosynyl residues are probably located at or near the inhibitor binding site.