• Journal of Microbiology
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• v.35 no.3
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• pp.193-199
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• 1997

From several industrial wastewaters, 14 bacterial strains which degrade benzene, toluene, o-xylene, m-xylene, or p-xylene (BTX) were obtained. These strains were characterized as to their species composition and the substrate range, kinetic parameters and the substrate interactions were investigated. Although BTX components have a similar chemical structure, isolated strains showed different substrate ranges and kinetic parameters. None of the strains could degrade all of BTX components and most of them showed an inhibition (Haldane) kinetics on BTX, BTX mixtures were removed under inhibitory substrate interactions with variation in the intensity of inhibition. For a complete degradation of BTX, a defined mixed culture containing three different types of patyways was constructed and all of the BTX components were simultaneously degraded with the totla removal rate of 225.69 mg/g biomass/h Judging from the results, the obtained mixed culture seems to be useful for the treatment of BTX-contaminated wastewater or groundwater as well as for the removal of BTX from the contaminated air stream.

• Journal of Applied Biological Chemistry
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• v.60 no.2
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• pp.173-178
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• 2017

This study was conducted to investigate the effect of pyroligneous acids on urea hydrolysis for the purpose of inhibiting ammonia volatilization during urea fertilizer application. Different types of synthetic urease inhibitors have been searched and developed, but their use is limited due to varying inhibition effects on soil urease, and environmental problems. In this study, the effect of pyroligneous acids, a natural substance, on urea hydrolysis in soil was evaluated by analyzing inhibition of urease activity. Pyroligneous acids inhibited plant urease and microbial urease activity, as well as soil urease with various urease complex. In addition, pyroligneous acids exhibited non-competitive urease inhibition effect through urease kinetics and inhibited urea hydrolysis in the soil. This study showed that pyroligneous acids treatment with urea fertilizer decreases the loss of urea fertilizer, improves the efficiency of nitrogen application on plant and reduces the amount of nitrogen fertilizers applied in soil.

• Proceedings of the PSK Conference
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• 2002.10a
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• pp.312.3-313
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• 2002

Recently we have reported that various hydroxystilbenes show strong inhibition of human P450 1 activity. A series of synthetic trans-stilbene derivatives were prepared and their inhibitory potentials were evaluated with the bacterial membrane of recombinant human P450 1A1, 1A2 or 1B1 coexpressed with human NADPH-P450 reductase to find new candidates for cancer chemoprevention, Of the compounds tested. SY-021 (3.5-dimethoxyphenyl vinyl thiophene) exhibited a potent inhibition of human P450 181 with an IC$_{50}$ value of 2 nM. SY-021 also showed the inhibitrion of P450 1A1 with IC$_{50}$ value of 61 nM and P450 1A2 with IC$_{50}$ value of 11 nM. SY-021 showed 31-fold selectivity for P450 1B1 over P450 1A1 and 6-fold selectivity for P450 1B1 over 1A2. We have further investigated the inhibition kinetics of P450 1A1. 1A2 and 1B1 by SY-021. The modes of inhibition by SY-021were non-compeitive for all three P450 1 enzymes. Effect of preincubation with NADPH on inhibition of P450 1B1 by SY-021 was determined. These results suggest that SY-021 is one of the mostj potent inhibitor of human P450 1 enzymes and may be considered as a good candidate for a cancer chemopreventive agent in human

• KSBB Journal
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• v.11 no.3
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• pp.276-287
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• 1996

Batch suspension cultures of hybridoma cell were performed with various initial glutamine concentrations to investigate the effects of glutamine on cell growth and death, monoclonal antibody production, glucose and glutamine consumption, and the production of lactate and ammonium ion. An mathematical kinetic model was formulated to describe the kinetics of cell growth, the consumption of nutrients (glucose and glutamine), and the production of monoclonal antibody and waste metabolites (lactate and ammonium ion) based on experimental data. An equation for the specific growth rate was developed such that superimposed Monod equation in glucose and glutamine, with non-competitive type inhibition relations in ammonium ion and lactate. The inhibition constant for lactate was inversely proportional to the lactate concentration. The specific death rate was considered to be a function of glucose, glutamine, ammonium ion and lactate concentration.

• BMB Reports
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• v.39 no.4
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• pp.394-399
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• 2006

The transport of putrescine into a moderately salt tolerant cyanobacterium Synechocystis sp. PCC 6803 was characterized by measuring the uptake of radioactively-labeled putrescine. Putrescine transport showed saturation kinetics with an apparent $K_m$ of $92{\pm}10\;{\mu}M$ and $V_{max}$ of $0.33{\pm}0.05\;nmol/min/mg$ protein. The transport of putrescine was pH-dependent with highest activity at pH 7.0. Strong inhibition of putrescine transport was caused by spermine and spermidine whereas only slight inhibition was observed by the addition of various amino acids. These results suggest that the transport system in Synechocystis sp. PCC 6803 is highly specific for polyamines. Putrescine transport is energy-dependent as evidenced by the inhibition by various metabolic inhibitors and ionophores. Slow growth was observed in cells grown under salt stress. Addition of low concentration of putrescine could restore growth almost to the level observed in the absence of salt stress. Upshift of the external osmolality generated by either NaCl or sorbitol caused an increased putrescine transport with an optimum 2-fold increase at 20 mosmol/kg. The stimulation of putrescine transport mediated by osmotic upshift was abolished in chloramphenicol-treated cells, suggesting possible involvement of an inducible transport system.

• YAKHAK HOEJI
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• v.38 no.2
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• pp.114-122
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• 1994

A study on the absorption mechanism of cefixime(CF), an oral ${\alpha}-amino$ group deficient cephalosporin antibiotic, has been undertaken through the rat jejunum and nasal cavity using an in situ simultaneous perfusion technique developed in our laboratory. CF was well absorbed in the jejunum and nasal cavity of rats at pH 5.0, but not at pH 7.0. CF absorption was studied over four orders of magnitude in concentration to determine saturability. Disappearance of CF in the perfusate followed first-order kinetics at all tested concentrations. The apparent first-order absorption rate constant was found to be dependent on the concentration over the range of $0.1\;mM{\sim}3\;mM$ in the jejunum and nasal cavity of rats. Inhibitors were added to determine the competitive inhibition of CF absorption. The presence of L-tyrosine, L-phenylalanine, alanine-alanine, glycine-glycine and cefadroxil produced the significant inhibition of CF absorption in the nasal cavity and jejunum. However, there was no evidence of the inhibition in the presence of cefazolin. In addition, The CF absorption in the nasal cavity and jejunum was inhibited significantly by ouabain and 2,4-dinitrophenol(DNP). This study suggested that CF is absorbed across the rat nasal cavity and jejunum by carrier-mediated transport mechanism and energy consuming system.

• Bulletin of the Korean Chemical Society
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• v.35 no.5
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• pp.1379-1384
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• 2014

${\alpha}-Fe_2O_3$ spherical particles having an average diameter of ca. 420 nm and ${\alpha}-Fe_2O_3$ fine particles (< 10 ${\mu}m$ particle size) were prepared to examine as catalysts for CO oxidation. Kinetic studies on the catalytic reactions were performed in a flow reactor using an on-line gas chromatography system operated at 1 atm. The apparent activation energies and the partial orders with respect to CO and $O_2$ were determined from the rates of CO disappearance in the reaction stage showing a constant catalytic activity. In the temperature range of $150-275^{\circ}C$, the apparent activation energies were calculated to be 13.7 kcal/mol on the ${\alpha}-Fe_2O_3$ spherical submicron clusters and 15.0 kcal/mol on the ${\alpha}-Fe_2O_3$ fine powder. The Pco and $Po_2$ dependencies of rate were investigated at various partial pressures of CO and $O_2$ at $250^{\circ}C$. Zero-order kinetics were observed for $O_2$ on both the catalysts, but the reaction order for CO was observed as first-order on the ${\alpha}-Fe_2O_3$ fine powder and 0.75-order on the ${\alpha}-Fe_2O_3$ spherical submicron clusters. The catalytic processes including the inhibition process by $CO_2$ on the ${\alpha}-Fe_2O_3$ spherical submicron powder are discussed according to the kinetic results. The catalysts were characterized using XRD (X-ray powder diffraction), FE-SEM (field emission-scanning electron microscopy), HR-TEM (high resolution-transmission electron microscopy), and $N_2$ sorption measurements.

• BMB Reports
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• v.38 no.5
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• pp.584-590
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• 2005

Glucose 6-phosphate dehydrogenase (EC 1.1.1.49) was purified from Aspergillus aculeatus, a filamentous fungus previously isolated from infected tongue of a patient. The enzyme, apparently homogeneous, had a specific activity of $220\;units\;mg^{-1}$/, a molecular weight of $105,000{\pm}5,000$ Dal by gel filtration and subunit size of $52,000{\pm}1,100$ Dal by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The substrate specificity was extremely strict, with glucose 6-phosphate (G6P) being oxidized by nicotinamide adenine dinucleotide phosphate (NADP) only. At assay pH of 7.5, the enzyme had $K_m$ values of $6\;{\mu}m$ and $75\;{\mu}m$ for NADP and G6P respectively. The $k_{cat}$ was $83\;s^{-1}$. Steady-state kinetics at pH 7.5 produced converging linear Lineweaver-Burk plots as expected for ternary-complex mechanism. The patterns of product and dead-end inhibition suggested that the enzyme can bind NADP and G6P separately to form a binary complex, indicating a random-order mechanism. The enzyme was irreversibly inactivated by heat in a linear fashion, with G6P providing a degree of protection. Phosphoenolpyruvate (PEP), adenosinetriphosphate (ATP), and fructose 6-phosphate (F6P), in decreasing order, are effective inhibitors. Zinc and Cobalt ions were effective inhibitors although cobalt ion was more potent; the two divalent metals were competitive inhibitors with respect to G6P, with $K_i$ values of $6.6\;{\mu}m$ and $4.7\;{\mu}m$ respectively. It is proposed that inhibition by divalent metal ions, at low NADPH /NADP ratio, is another means of controlling pentosephosphate pathway.

• Bulletin of the Korean Chemical Society
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• v.15 no.5
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• pp.394-399
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• 1994

The catalytic mechanism of malonyl-CoA synthetase from Rhizobium trifolii was investigated by the steady state kinetics and intermediate identification. Initial velocity studies and the product inhibition studies with AMP and PPi strongly suggested ordered Bi Uni Uni Bi Ping-Pong Ter Ter system as the most probable steady state kinetic mechanism of malonyl-CoA synthetase. Michaelis constants were $0.17{\pm}0.04 {\mu}M,\;0.24{\pm}0.18 {\mu}M\;and\;0.045{\pm}0.26 {\mu}$M for ATP, malonate and CoA, respectively. The TLC analysis of the $^{32}P-labelled$ products in reaction mixture containing $[{\gamma}-^{32}P]$ ATP in the absence of CoA showed that PPi was produced after the sequential addition of ATP and malonate. Formation of malonyl-AMP, suggested as an intermediate in the kinetically deduced mechanism, was confirmed by the analysis of $^{31}P-NMR$ spectra of AMP product isolated from the $^{18}O$ transfer experiment using $[^{18}O]$malonate. Two resonances were observed, corresponding to AMP labelled with zero and one atom of $^{18}O$, indicating that one atom of $^{18}O$ transferred from $[^{18}O]$malonate to AMP through the formation of malonyl-AMP. Formation of malonyl-AMP was also confirmed through the TLC analysis of reaction mixture containing $[{\alpha}-^{32}P]$ATP. These results strongly support the ordered Bi Uni Uni Bi Ping-Pong Ter Ter mechanism deduced from the initial velocity and product inhibition studies.

• BMB Reports
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• v.54 no.6
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• pp.311-316
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• 2021

Ethanol often causes critical health problems by altering the neuronal activities of the central and peripheral nerve systems. One of the cellular targets of ethanol is the plasma membrane proteins including ion channels and receptors. Recently, we reported that ethanol elevates membrane excitability in sympathetic neurons by inhibiting Kv7.2/7.3 channels in a cell type-specific manner. Even though our studies revealed that the inhibitory effects of ethanol on the Kv7.2/7.3 channel was diminished by the increase of plasma membrane phosphatidylinositol 4,5-bisphosphate (PI(4,5)P₂), the molecular mechanism of ethanol on Kv7.2/7.3 channel inhibition remains unclear. By investigating the kinetics of Kv7.2/7.3 current in high K⁺ solution, we found that ethanol inhibited Kv7.2/7.3 channels through a mechanism distinct from that of tetraethylammonium (TEA) which enters into the pore and blocks the gate of the channels. Using a non-stationary noise analysis (NSNA), we demonstrated that the inhibitory effect of ethanol is the result of reduction of open probability (P_O) of the Kv7.2/7.3 channel, but not of a single channel current (i) or channel number (N). Finally, ethanol selectively facilitated the kinetics of Kv7.2 current suppression by voltage-sensing phosphatase (VSP)-induced PI(4,5)P₂ depletion, while it slowed down Kv7.2 current recovery from the VSP-induced inhibition. Together our results suggest that ethanol regulates neuronal activity through the reduction of open probability and PI(4,5)P₂ sensitivity of Kv7.2/7.3 channels.