• Journal of Oral Medicine and Pain
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• v.34 no.3
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• pp.227-235
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• 2009

Many of the protective functions of saliva can be attributed to the biological, physical, structural, and rheological characteristics of salivary glycoproteins. Therefore, the development of ideal saliva substitutes requires understanding of the rheological as well as biological properties of human saliva. In the present study, we investigated the changes of salivary enzymatic activities by saliva substitutes and compared viscosity of saliva substitutes with human saliva. Five kinds of saliva substitutes such as Moi-Stir, Stoppers4, MouthKote, Saliva Orthana, and SNU were used. Lysozyme activity was determined by the turbidimetric method. Peroxidase activity was determined with an NbsSCN assay. $\alpha$-Amylase activity was determined using a chromogenic substrate, 2-chloro-p-nitrophenol linked with maltotriose. The pH values of saliva substitutes were measured and their viscosity values were measured with a cone-and-plate digital viscometer at six different shear rates. Various types of saliva substitutes affected the activities of salivary enzymes in different ways. Stoppers4 enhanced the enzymatic activities of hen egg-white lysozyme, bovine lactoperoxidase (bLP), and $\alpha$-amylase. Saliva Orthana and SNU inhibited bLP activity and enhanced $\alpha$-amylase activity. MouthKote inhibited $\alpha$-amylase activity. Moi-Stir inhibited the enzymatic activities of bLP and $\alpha$-amylase. The pH values were very different according to the types of saliva substitutes. Stoppers4, MouthKote, and Saliva Orthana showed lower values of viscosity at low shear rates and higher values of viscosity at high shear rates compared with unstimulated and stimulated whole saliva. Moi-Stir and SNU displayed much higher values of viscosity than those of natural whole saliva. Collectively, our results indicate that each saliva substitute has its own biological and rheological characteristics. Each saliva substitute affects the enzymatic activity of salivary enzyme and finally oral health in different ways.

• Toxicological Research
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• v.6 no.1
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• pp.51-59
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• 1990

Effects of altering hepatic mixed-function oxidase (MFO) enzyme activities on the metabolism and acute toxicity of parathio were investigated in adult female rats. In vitro hepatic metabolism of parathion to paraoxon was increased by phenobarbital pretreatment (50 mg/kg/day, ip, for 4 consecutive days) and SKF 525-A (50 mg/kg, ip, 1 hr prior to sacrifice) decreased paraoxon formation indicating that phenobarbital induces that form(s) of cytochrome P-450 catalyzing conversion of parathion to paraoxon. Degradation of paraoxon to p-nitrophenol was increased by phenobarbital pretreatment, but not affected by SKF 525-A suggesting that MFO activities play only a minor role in the detoxification of the active metabolite of this insecticide. The phenobarbital-induced increase in paraoxon formation was partially antagonized by SKF 525-A. Significant activity for both parathion activation and paraoxon degradation was also observed in the lung preparation, however, this extrahepatic parathion and paraoxon metabolizing activity was not induced by phenobarbital or inhibited by SKF 525-A pretreatment. Phenobarbital pretreatment increased paraoxon level in livers of rats when measured 3 hr following parathion injection (2 mg/kg, ip). SKF 525-A did not alter parathion or paraoxon levels in brain, blood and liver. Phenobarbital pretreatment decreased the toxicity of parathion (4mg/kg, ip) or paraoxon (1.5 mg/kg, ip) as determined by decreases in lethality and inhibition of brain and lung acetylcholinesterases. An additional SKF 525-A treatment failed to decrease the protective effects of phenobarbital against parathion or paraoxon toxicity. These results suggest that some unknown factors other than hepatic MFO induction are involved in the protective action of phenobarbital against parathion and paraoxon toxicity.

• Journal of Life Science
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• v.12 no.6
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• pp.803-811
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• 2002

The present study was carried out for research and development of natural antimicrobial from extract of Stachys sieboldii MIQ against food borne bacteria. The hexane extract of Stachys sieboldii MIQ at 250$\mu\textrm{g}$/$m\ell$ per disc showed 15 ~ 20 mm inhibition zone against gram positive and gram negative barteria. Minimum inhibitory concentration (MIC) of hexane extract was 250${\mu}g$/$m\ell$against Bacillus cereus, 250~500${\mu}g$/$m\ell$against Listeria monocytogenes, 500${\mu}g$/$m\ell$ against Staphylococcus aureus, Psedomonas aeruginosa. Observation by transmission electron microscope, showed that disruption of the cell wall assumed to be due to the bactericidal activity. In addition, the membrane integrity of the sensitive cells was disrupted by exposure to Stachys sieboldii MIQ extract on the D-$\beta$-galatosidase activity as substrate of O-nitrophenol-$\beta$-D-galacto-pyranoside. The hexane extract of Stachys sieboldii MIQ was very stable on the pH and thermal stability.

• Biomolecules & Therapeutics
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• v.23 no.2
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• pp.201-206
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• 2015

Scutellaria baicalensis is one of the most widely used herbal medicines in East Asia. Because baicalein and baicalin are major components of this herb, it is important to understand the effects of these compounds on drug metabolizing enzymes, such as cytochrome P450 (CYP), for evaluating herb-drug interaction. The effects of baicalin and baicalein on activities of ethoxyresorufin O-deethylase (EROD), methoxyresorufin O-demethylase (MROD), benzyloxyresorufin O-debenzylase (BROD), p-nitrophenol hydroxylase and erythromycin N-demethylase were assessed in rat liver microsomes in the present study. In addition, the pharmacokinetics of caffeine and its three metabolites (i.e., paraxanthine, theobromine and theophylline) in baicalin-treated rats were compared with untreated control. As results, EROD, MROD and BROD activities were inhibited by both baicalin and baicalein. However, there were no significant differences in the pharmacokinetic parameters of oral caffeine and its three metabolites between control and baicalin-treated rats. When the plasma concentration of baicalin was determined, the maximum concentration of baicalin was below the estimated $IC_{50}$ values observed in vitro. In conclusion, baicalin had no effects on the pharmacokinetics of caffeine and its metabolites in vivo, following single oral administration in rats.

• Journal of the Korean Chemical Society
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• v.39 no.12
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• pp.918-924
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• 1995

THMs and PCBs were separated and analysed with elution on Novapak ODS or $\mu-Bondapak$ phenyl column by an eluent containing p-nitrophenol (p-NP). THMs studied were CHCl3, CHBrCl2, CHBr2Cl, and CHBr3, and PCBs used were Aroclor 1221, 1242, 1248, $\alpha-$ and $\beta-BHC.$ It was thought that the retention on the stationary phase and sensitivities of the samples are related to the interaction between the sample and stationary phase or p-NP. THMs were separated completely on the ODS column by elution with MeOH-water (30 : 70) containing $1.0{\times}10^{-4}$ M p-NP and some of PCBs were separated on the phenyl column by elution with $CH_3CN$-water(50 : 50) containing $1.0{\times}10^{-4}$ M p-NP. Detection limits of THMs were from $1.0{\times}10^{-4}$ g to $1.0{\times}10^{-6}$ g. Aroclors were $2{\times}10^{-6}$ g, and $\alpha-$ and $\beta-BHC$ were $2{\times}10^{-4}$ g and $1.0{\times}10^{-4}$ g respectively.

• Journal of Microbiology and Biotechnology
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• v.24 no.6
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• pp.771-780
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• 2014

A putative lipolytic enzyme gene, named as est9x, was obtained from a marine microbial metagenome of the South China Sea. Sequence analysis showed that Est9X shares lower than 27% sequence identities with the characterized lipolytic enzymes, but possesses a catalytic triad highly conserved in lipolytic enzymes of the ${\alpha}/{\beta}$ hydrolase superfamily. By phylogenetic tree construction, Est9X was grouped into a new lipase/esterase family. To understand Est9X protein in depth, it was recombinantly expressed, purified, and biochemically characterized. Within potential hydrolytic activities, only lipase/esterase activity was detected for Est9X, confirming its identity as a lipolytic enzyme. When using p-nitrophenol esters with varying lengths of fatty acid as substrates, Est9X exhibited the highest activity to the C2 substrate, indicating it is an esterase. The optimal activity of Est9X occurred at a temperature of $65^{\cric}C$, and Est9X was pretty stable below the optimum temperature. Distinguished from other salt-tolerant esterases, Est9X's activity was tolerant to and even promoted by as high as 4 M NaCl. Our results imply that Est9X is a unique esterase and could be a potential candidate for industrial application under extreme conditions.

• Journal of The Korean Society of Clinical Toxicology
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• v.16 no.1
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• pp.1-8
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• 2018

Purpose: Extremely hazardous pesticides are classified as World Health Organization (WHO) hazard class Ia. However, data describing the clinical course of WHO class Ia OP (organophosphate) poisonings in humans are very scarce. Here, we compare the clinical features of patients who ingested hazard class Ia OPs. Methods: This retrospective observational case study included 75 patients with a history of ingesting ethyl p-nitrophenol thio-benzene phosphonate (EPN), phosphamidon, or terbufos. The patients were divided according to the chemical formulation of the ingested OP. Data regarding mortality and the development of complications were collected and compared among groups. Results: There were no differences in the baseline characteristics and severity scores at presentation between the three groups. No fatalities were observed in the terbufos group. The fatality rates in the EPN and phosphamidon groups were 11.8% and 28.6%, respectively. Patients poisoned with EPN developed respiratory failure later than those poisoned with phosphamidon and also tended to require longer mechanical ventilatory support than phosphamidon patients. The main cause of death was pneumonia in the EPN group and hypotensive shock in the phosphamidon group. Death occurred later in the EPN group than in the phosphamidon group. Conclusion: Even though all three drugs are classified as WHO class Ia OPs (extremely hazardous pesticides), their clinical courses and the related causes of death in humans varied. Their treatment protocols and predicted outcomes should therefore also be different based on the chemical formulation of the OP.

• Analytical Science and Technology
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• v.17 no.5
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• pp.393-400
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• 2004

Nitrosation of phenol (POH) was studied by adding hydrochloric acid and sodium nitrite to phenol solution with reaction temperature and time change. The optimum condition of nitrosation was found from the effects of hydrochloric acid and sodium nitrite concentration, reaction temperature, and reaction time changes on the production of nitrosophenol (POHNO). As a result, it was found that the optimum conditions were $5.0{\times}10^{-4}{\sim}2.0{\times}10^{-3}M$ range of $NO{_2}^-$ concentration, more than 0.10 M of HCl concentration, temperature of $80^{\circ}C$, and 3 hrs. of reaction time. In this condition, 10 U.S. E.P.A. classified priority environmental pollutant, phenols, were nitrosated. Nitrosated phenols were: POH, 2-Chlorophenol (2ClPOH), 2,4-diChlorophenol (2ClPOH), 2,4-dimethylphenol (24diMPOH), and 4-Chloro -3-methylphenol (4Cl3MPOH), and a small part of 2-nitrophenol (2NPOH). The ${\lambda}_{max}$ values of nitrosated phenols in acidic solution were around 300 nm, and those in basic solution were around 400 nm. Molar absorptivities (${\varepsilon}$) at the 400 nm of the nitrosated phenols in the basic solution were 1.5~2.0 times larger than those at 300 nm in acidic solution. It was also found by Capillary-HPLC chromatograms of the nitrosated phenol solutions that the production of the nitrosophenols were interfered by the excess concentration of nitrite (more than $3.0{\times}10^{-3}M$).

• Microbiology and Biotechnology Letters
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• v.42 no.4
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• pp.347-353
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• 2014

${\beta}$-Glucosidase from Aspergillus usamii KCTC 6954 was used to convert ginsenoside Rb1 to compound K, which has a high bio-functional activity. The enzymatic activities during culturing for 15 days were determined using ${\rho}$-nitrophenyl-${\beta}$-glucopyranoside. The growth rate of the strain and the enzymatic activity were maximized after 6 days (IU; $175.93{\mu}M\;ml^{-1}\;min^{-1}$). The activities were maximized at $60^{\circ}C$ in pH 6.0. During culturing, Rb1 was converted to Rd after 9 d and then finally converted to compound K at 15 d. In the enzymatic reaction, Rb1 was converted to the ginsenoside Rd within 1 h of reaction time and compound K could be detected after 8 h. As a result, this study demonstrates that $Rb1{\rightarrow}Rd{\rightarrow}F2{\rightarrow}$compound K is the main metabolic pathway catalyzed by ${\beta}$-glucosidase and that ${\beta}$-glucosidase is a feasible option for the development of specific bioconversion processes to obtain minor ginsenosides such as Rd and compound K.

• Microbiology and Biotechnology Letters
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• v.40 no.1
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• pp.1-9
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• 2012

This study's aim was to isolate microorganisms producing agarase with a high activity, with possible applications in improving the performance of the pretreatment processes for bioethanol production. Marine algaes were collected from the south coast of Korea, from which three kinds of microorganisms were isolated. After a 4-day culture of these strains at $25^{\circ}C$, crude enzymes were obtained from culture supernatant or cell-free extract by ammonium sulfate precipitation and membrane dialysis. Agarase activity was observed in these crude enzymes. Notably higher specific activity was observed in the crude enzyme obtained from the culture supernatant rather than that from the cell-free extract. This indicates that a secreted enzyme has a much greater activity than a cellular enzyme. Crude enzymes from the GNUM08122 strain were inferred to have ${\alpha}$-agarase activity because release of p-nitrophenol was observed, possibly due to the cleavage of p-nitrophenyl-${\alpha}$-D-galactopyranoside. The 16S rRNA sequence of GNUM08122 showed a close relationship to Pseudoalteromonas issachenkonii KMM 3549 (99.8%) and Pseudoalteromonas tetraodonis IMA 14160 (99.7%), which led us to assign it to the genus Pseudoalteromonas. Biochemical and physiological study revealed that this strain can grow well at $40^{\circ}C$ under a wide range of pH (pH 4~8) in high-salt conditions (10% NaCl).