• Korean Journal of Environmental Agriculture
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• v.28 no.4
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• pp.453-461
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• 2009

Killifish (Oryzias latipes) were exposed to an organophosphate pesticide, pirimiphos-methyl, in a flow-through system to determine the bioconcentration factor (BCF) following GLP (Good Laboratory Practice). This study was conducted at two different concentrations (1 and $10\;{\mu}$g/L) of $^{14}C$-labeled pirimiphos-methyl for 28 days uptake and 14 days depuration according to the OECD 305 test guideline. The $BCF_{ss}$ for total radioactive residues in whole fish were 1,251 and 1,277 for low and high concentrations, respectively. The $BCF_k$ based on the uptake and depuration rate constants were 1,200 for both low and high concentrations. During the depuration phase, the accumulated test substance was rapidly depurated from fish. Greater than 95% of the residue at steady-state was depurated after 2 days. Although the measured BCF values were high, pirimiphos-methyl could be evaluated as a low risk from bioaccumulation by aquatic organisms due to the short depuration period and low amount of bound residue (1.5%). We suggest that in evaluating bioaccumulation, not only the BCF should be considered, but also depuration time and bound residue in aquatic organisms give an indication of the potential environmental risks.

• Archives of Pharmacal Research
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• v.19 no.5
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• pp.423-428
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• 1996

Optimum conditions for hydrolysis were investigated to enhance water-solubilities of protein-bound polysaccharides in the basidiocarps of Ganoderma lucidum by treating chymotrypsin. We also attempted with Ganoderma lucidum residue remaining after extracting hot water-soluble compoents in Ganoderma lucidum. After hydrolyzing under optimum conditions (20 ppm chymotrypsin, 2% Gampderma lucidum or 6% Ganoderma lucidum residue, at pH 10 and at $ 40^{\circ}C$), the amounts of total protein and carbohydrate of hydrolysate were measured. Michaelis constant, $K_{m}$, and maximum rate, $V_{max}$, calculated by Lineweaver-Buck plot for the hydrolysis of Ganoderma lucidum were 1.73% and 0.073%/min respectively and those for hydrolysis of Ganoderma lucidum residue were 2.40% and 0.033%/min respectively. The amount of polysaccharide isolated from Ganoderma lucidum (100 g) treated with chymotrypsin was only 3.07 g, but significantly increased amount (14.34 g) of polysaccharides was isolated from Ganoderma lucidum residue (100 g) treated with chymotrypsin. The protein-bound polysaccharide was isolated from the non-hydrolyzed and hydrolyzed sample and molecular weights of the polysaccharide were measured by Sepharose CL-48 gel filtration.

• The Korean Journal of Pesticide Science
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• v.2 no.3
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• pp.90-95
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• 1998

Soil residues of paraquat (1,1-dimethyl-4,4-dipyridinium dichloride) were determined in apple, pear, grape, and peach orchards for which 15 sites each were selected randomly from the corresponding large-scale production area throughout the country. Strong adsorption capacity measured using wheat bioassay (paraquat concentration required to reduce 50% root growth of wheat, SAC-WB) was also investigated on the orchard soils and the paraquat residue level was calculated against total SAC-WB values (SAC-WB value + paraquat residue). Average bound residue of paraquat on the 60 sites was 6.9 ppm, while paraquat residue in apple orchard reached 20.2 ppm which was the highest among the orchards and was almost double as compared with those in the other three orchards. Loosely bound residue of paraquat determined on the bound residue high top five soils occurred less than 0.5 ppm detection limit. Average SAC-WB value was 276.1 ppm and there were no any correlations between the SAC-WB value and clay content, organic matter content, and cation exchange capacity of the orchard soils. Paraquat residue level of the orchard soils against total SAC-WB recorded 2.43%.

• Korean Journal of Environmental Agriculture
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• v.10 no.2
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• pp.149-157
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• 1991

In order to elucidate the possible change in the non-extractable bound residue of TCAB(3,3' 4,4' - tetrachloroazobenzene) in soil as a function of aging period, uniformly ring-labelled $^{14}C-TCAB$ was treated to soil(organic matter : 1.8%), and aged for 3, 6, 9, 12 and 15 months at $21{\pm}1^{\circ}C$, respectively. $^{14}CO_2$ evolution and volatilization loss during the aging were negligible. The amounts of non-extractable bound residue of TCAB increased gradually from 7.55% in 3-month aging to 19.32% in 15-month aging. Partition data suggested no formation of polar groups in the chemical structure of TCAB. Most of $^{14}C-radioactivity$ of bound residues was present in humin in the range of 50.52 to 58.93%. The fact that the number of microorganisms in soil decreased relative to the control suggested no chance of their involvement in the formation of non-extractable bound residues. Accordingly, the increase in the non-extractable bound residue of TCAB in soil with aging period is believed to be due to the transformation of the trans isomer to the cis one which is more polar and more adsorptive than the former.

• Bulletin of the Korean Mathematical Society
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• v.55 no.3
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• pp.921-935
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• 2018

In this study we determine the structure of m-adic residue codes over the non-chain ring $F_q[v]/(v^2-v)$ and present some promising examples of such codes that have optimal parameters with respect to Griesmer Bound. Further, we show that the generators of m-adic residue codes serve as a natural and suitable application for generating reversible DNA codes via a special automorphism and sets over $F_{4^{2k}}[v]/(v^2-v)$.

• Archives of Pharmacal Research
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• v.15 no.3
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• pp.229-233
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• 1992

The pKa value of histidine-51 residue was determined by the pH dependency of contents of NADH bound to the active site in the orse liver alcohol dehydrogenase and % inactivation with diethyl pyrocarbonate treatment of the enzyme. The pKa for His-51 was -7.15 in the ternary complex and -6.7 in the enzyme itself.

• Journal of Hydrogen and New Energy
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• v.24 no.1
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• pp.44-49
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• 2013

Hydrogen penetration into a metal leads to damages and mechanical degradations and its content measurement is of importance. For a precise measurement, a sample preparation procedure must be optimized through a series of studies on sample washing and drying. In this study, two-step washing with organic solvents and thermal soaking in inert gas were tried with a rod-shaped, API X65 steel sample. The samples were machined from a steel plate and then washed in acetone and etyl-alcohol for 5 minute each and dried with compressed air. After then, the samples were thermally soaked in a home-made nitrogen gas chamber during 10 minute at different heat gun temperatures from 100 to $400^{\circ}C$ and corresponding temperature range in the soaking chamber was from 77 to $266^{\circ}C$ according to the temperature calibration. Hydrogen residue in the samples was measured with a hot extraction system after each soaking step; hydrogen residue of $0.70{\pm}0.12$ wppm after the thermal soaking at $77^{\circ}C$ decayed with increase of the soaking temperature. By adopting the heat transfer model, decay behavior of the hydrogen residue was fitted into an exponential decay function of the soaking temperature. Saturated value or lower bound of the hydrogen residue was 0.36 wppm and chamber temperature required to lower the hydrogen residue about 95% of the lower bound was $360^{\circ}C$. Furthermore, a thermal desorption spectroscopy was done for the fully soaked samples at $360^{\circ}C$. Weak hydrogen peak was observed for whole temperature range and it means that hydrogen-related contaminants of the sample surface are steadily removed by heating. In addition, a broad peak found around $400^{\circ}C$ means that parts of the hydrogen residue are irreversibly trapped in the steel microstructure.

• Archives of Pharmacal Research
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• v.19 no.4
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• pp.326-334
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• 1996

We investigated the optimum conditions for conversion of water-insoluble components of basidiocarps of Ganoderma lucidum to water-soluble components by hydrolyzing with chitinase. We also tried it with Ganoderma luciclum residue remaining after extracting hot water-soluble components of Ganoderma lucidum. After hydrolyzing under optimum conditions (20 ppm chitinase, 2% Ganoderma lucidum or 6% Ganoderma lucidum residue, at pH 3 and at $ 35^{\circ}C$), the contents of total water-soluble components (polysaccharide or protein) were measured, and it was found that the contents of water-soluble components increased to 1.5-2.7 fold. Michaelis constant, $K_m$ and maximum rate, $V_max$ calculated by Lineweaver-Burk plot for hydrolysis of Ganoderma lucidum were 1.75% and 0.02%/min respectively and those for hydrolysis of Ganoderma lucidum residue were 53.15% and 0.53%/min respectively The protein-bound polysaccharide was isolated after hydrolysis and molecular weights were measured by Sepharose CL-4B gel filtration and compared with the molecular weights of polysaccharide before hydrolysis.

• Molecules and Cells
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• v.42 no.8
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• pp.597-603
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• 2019

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a core enzyme of the aerobic glycolytic pathway with versatile functions and is associated with cancer development. Recently, Kornberg et al. published the detailed correlation between GAPDH and di- or monomethyl fumarate (DMF or MMF), which are well-known GAPDH antagonists in the immune system. As an extension, herein, we report the crystal structure of MMF-bound human GAPDH at $2.29{\AA}$. The MMF molecule is covalently linked to the catalytic Cys152 of human GAPDH, and inhibits the catalytic activity of the residue and dramatically reduces the enzymatic activity of GAPDH. Structural comparisons between $NAD^+$-bound GAPDH and MMF-bound GAPDH revealed that the covalently linked MMF can block the binding of the $NAD^+$ cosubstrate due to steric hindrance of the nicotinamide portion of the $NAD^+$ molecule, illuminating the specific mechanism by which MMF inhibits GAPDH. Our data provide insights into GAPDH antagonist development for GAPDH-mediated disease treatment.

• Molecules and Cells
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• v.43 no.8
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• pp.694-704
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• 2020

HslUV is a bacterial heat shock protein complex consisting of the AAA+ ATPase component HslU and the protease component HslV. HslV is a threonine (Thr) protease employing the N-terminal Thr residue in the mature protein as the catalytic residue. To date, HslUV from Gram-negative bacteria has been extensively studied. However, the mechanisms of action and activation of HslUV from Gram-positive bacteria, which have an additional N-terminal sequence before the catalytic Thr residue, remain to be revealed. In this study, we determined the crystal structures of HslV from the Gram-positive bacterium Staphylococcus aureus with and without HslU in the crystallization conditions. The structural comparison suggested that a structural transition to the symmetric form of HslV was triggered by ATP-bound HslU. More importantly, the additional N-terminal sequence was cleaved in the presence of HslU and ATP, exposing the Thr9 residue at the N-terminus and activating the ATP-dependent protease activity. Further biochemical studies demonstrated that the exposed N-terminal Thr residue is critical for catalysis with binding to the symmetric HslU hexamer. Since eukaryotic proteasomes have a similar additional N-terminal sequence, our results will improve our understanding of the common molecular mechanisms for the activation of proteasomes.