• The Korean Journal of Zoology
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• v.4 no.1
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• pp.7-12
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• 1961

1) Respiratory metabolism patterns and its enzyme systems in the gill tissue of the fresh water mussels, Cristaria plicata were investigated through the examination on the effects of respiratory enzyme inhibitors, (KCN, NAF) and succinoxidase assay, while studying the effects of neutral salts (NaCL, KCL, CaCl2) and pH on oxygen consumption of the gill tissue. 2) In the limited concentration of KCL (0.3mM) and NaCl (0.4mM) solutions, oxygen consumption of the intact gill tissue was accelerated, but in CaCl2(0.5mM) solution, it showed no significant effect. The oxygen consumption was gradually decreased at the above concentrations of these limitations. The optimum pH for the respiration of the gill was 7.3. 3)Cyanide in 10-8M solution inhibited 88.8% of the respiration of the intact gill tissue. Methylene blue accelerated the respiration of the noral gill tissue, and slightly but significantly reversed the cyaniide poisoned respiration. 4)Oxygen consumption of the gill homogenate was apparently increased by the mixed addition of succinate, cytochrome c and activators (AlCl3 and CaCl2). This results suggested that succinoxidase system acts on the respiratory pattern of the gil tissue. 5) It was able to recognize that the enolase, which acts on the anaerobic glycolytic system, participated in the tissue respiration of the gill for NaF in 5$\times$10-2 M solution inhibited 55.5% of the respiration of the same intact tissue.

• Journal of Microbiology and Biotechnology
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• v.17 no.5
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• pp.761-768
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• 2007

Serratia proteamaculans HY-3 isolated from the digestive tract of a spider produces an extracellular protease named arazyme, with an estimated molecular mass of 51.5 kDa. The purified enzyme was characterized as having high activities at wide pH and temperature ranges. We further characterized biochemical features of the enzymatic reactions under various reaction conditions. The protease efficiently hydrolyzed a broad range of protein substrates including albumin, keratin, and collagen. The dependence of enzymatic activities on the presence of metal ions such as calcium and zinc indicated that the enzyme is a metalloprotease, together with the previous observation that the proteolytic activity of the enzyme was not inhibited by aspartate, cysteine, or serine protease inhibitors, but strongly inhibited by 1,10-phenanthroline and EDTA. The araA gene encoding the exoprotease was isolated as a 5.6 kb BamHI fragment after PCR amplification using degenerate primers and subsequent Southern hybridization. The nucleotide sequence revealed that the deduced amino acid sequences shared extensive similarity with those of the serralysin family of metalloproteases from other enteric bacteria. A gene(inh) encoding a putative protease inhibitor was also identified immediately adjacent to the araA structural gene.

• Parasites, Hosts and Diseases
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• v.38 no.3
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• pp.159-166
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• 2000

The present study intended to verify activities of cysteine proteinase of Pneumocystis carinii from rats and to purify the enzyme. In order to exclude the contamination of host-derived enzymes, concentrates of P. carinii was primarily treated with a mixture of proteinase inhibitors before Iysis of P carinii. A 68-kDa cysteine proteinase was finally purified from the crude extract of P. carinii by 4 sequential chromatographic methods. The enzyme showed an optimal activity at pH 5.5 in 0.1 M sodium acetate, and its activity was specifically inhibited by L-trans-epoxy-succinylleucylamido (4-guanidino) butane (E-64) and iodoacetic acid, suggesting that the enzyme is a cysteine proteinase. The 68-kDa proteinase weakly digested rnacrornolecules such as collagen, hemoglobin and fibronectin. The present study demonstrated the activity of cysteine proteinase at the 68-kDa band of P. carinii, and purified and characterized the molecule.

• Journal of the Korean Society of Food Science and Nutrition
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• v.12 no.4
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• pp.316-322
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• 1983

In order to obtain elementary data of enzymatic browning of apples and apple products and to examine effectively inhibitory method of browning, we extracted polyphenol oxidase (EC 1.10.3.1) from apple (Ralls Janet) and investigated its general properties. The optimum conditions for the enzyme reaction were pH 6.0 and temperature of $30^{\circ}C$. The enzyme was very stable at pH 4.0, and at the range of pH 5.0-9.0 its activity was above 80% compared with pH 4.0. The enzyme was very stable by heating at $40^{\circ}C$ for 1 hour, and almost 50% of enzyme activity was lost by heating at $60^{\circ}C$ for 30 minutes. The polyphenol oxidase activity was enhanced by the addition of $Cu^{2+}$ and $Mn^{2+}$, respectively, meanwhile $Na^+$, $Hg^{2+}$ and $Co^{2+}$ inhibited the enzyme activity. The enzyme activity was greatly decreased in the presence of inhibitors such as cysteine, sodium metabisulfite and ascorbic acid. The polyphenol oxidase greatly catalyzed the oxidation of o-diphenols such as chlorogenic acid and catechol, which suggests that main substrate of polyphenol oxidase is o-diphenol compounds.

• Bulletin of the Korean Chemical Society
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• v.32 no.spc8
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• pp.3022-3030
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• 2011

Since the discovery of the fact that compounds bearing a vinylic fluoride moiety often exhibit remarkable biological activities such as enzyme inhibitors, many synthetic methods for fluorine-substituted vinylic compounds have been developed. The synthesis of selectively fluorinated building blocks, such as arylsubstituted fluoro-alkenes, also has become an area of interest in recent years. Herein we describe a novel and practical method for the synthesis of 1,1-difluoro- and 1-fluoroalkenes starting from easily accessible trifluoroacetophenone derivatives. Various 1,1-difluoro- and 1-fluoroalkenes were prepared by the reaction of the corresponding tosyl hydrazones that were derived from trifluoroacetophenone derivatives by treating with alkyl or aryllithium reagents via addition-elimination and single electron transfer (SET) mechanism.

• YAKHAK HOEJI
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• v.46 no.6
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• pp.387-391
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• 2002

In vitro $\beta$-lactamase inhibitory activity of 6-exomethylene sulbactam compounds (CH-120, 130, 140, 145, 150, 155) was compared with clavulanic acid, sulbactam and tazobactam. The inhibitory activity of CH-140 was stronger than sulbactam and clavulanic acid against Type II, III, IV, TEM enzymes and stronger than tazobactam against Type IV enzyme. The inhibitory activity of CH-145 was stronger than sulbactam and clavulanic acid against Type I, II, III, IV, TEM enzymes and stronger than tazobactam against Type III, IV enzymes. The in vitro antimicrobial activity of CH-140 and CH-145 combined with piperacillin and ceftriaxone was compared with the sulbactam and tazobactam against $\beta$-lactamase producing 31 strains. But, synergistic activity of CH-140 and CH-145 was inferior to tazobactam.

• BMB Reports
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• v.30 no.3
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• pp.182-187
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• 1997

The NADPH oxidase of phagocytes catalyzes the reduction of oxygen to $O_2^-$ at the expense of NADPH. The enzyme is dormant in resting neutrophils and becomes activated on stimulation. During activation, $p47^{phox}\;(\underline{ph}agocyte\;\underline{ox}idase\;factor)$, a cytosolic oxidase subunit, becomes extensively phosphorylated at a number of serines located between S303-S379. Oxidase activation can also be achieved by the addition of phosphorylated recombinant $p47^{phox}$ by protein kinase C in the cell-free system in the presence of $GTP{\gamma}S$. The cell-free activation is inhibited by wortmannin and LY294002. specific inhibitors of phosphatidylinositol 3kinase (PI 3-kinasel) These results indicate that PI 3-kinase may playa pivotal role in the activation of NADPH oxidase.

• Journal of Life Science
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• v.9 no.4
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• pp.408-413
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• 1999

Extracellular capsidiol, sesquiterpenoid phytoalexin, in the medium of pepper (Capsicum annuum L.) suspension cells was not identified from control cells, but highly accumulated in the elicitor-induced cells within 6 hours after the addition of 0.05$\mu\textrm{g}$/$m\ell$ cellulase. Capsidiol production in elicitor-induced cells was markedly suppressed by cytochrome P450 inhibitors, such as ancymidol and ketoconazole demonstrating that biosynthesis of capsidiol is catalyzed by at least on hydroxylation enzyme in the biochemical pathway. Based on protein electrophoresis, two bands, 23.0kDa and 27.5kDa, were identified as newly synthesized polypeptides in the elicitor-induced suspension cells, suggesting that pepper cells which were subjected to elicitor treatment activate specific gene(s) for capsidiol biosynthesis in cultured cells.

• Journal of the Korea Institute of Military Science and Technology
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• v.14 no.5
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• pp.920-931
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• 2011

Nerve agents are irreversible inhibitors of the cholinesterase enzyme. Exposure causes a progression of toxic signs, including hypersecretions, fasciculations, tremor, convulsions, respiratory distress, epileptiform seizures, brain injuries and death. A combined regimen of prophylaxis and therapy is the most effective medical countermeasure for dealing with the threat of nerve agent poisoning to military personnel. In this paper, the author investigated the updated technologies regarding various pre- and post-treatment drugs for nerve agents detoxification which are under development in several countries including Korea. Some characteristics of active ingredients in the formulations of drugs, their action mechanisms, and effectiveness were analyzed. Additionally, part of experimental data on the transdermal patch studied in ADD using beagle dogs was introduced.

• Natural Product Sciences
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• v.6 no.1
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• pp.36-39
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• 2000

Acorenone, a diterpene isolated from Acorus gramineus, showed strong resistance inhibitory activity against multi-drug resistant microorganisms such as Staphylococcus aureus SA2, which has resistance to 10 usual antibiotics including chloramphenicol (Cm). At the level of $5\;{\mu}g/ml$ when combined with $50\;{\mu}g/ml$ of Cm. Bacterial resistance to Cm is due to the presence in resistant bacteria of an enzyme, chloramphenicol acetyltransferase (CAT), which catalyses the acetyl-CoA dependent acetylation of the antibiotic at C-3 hydroxyl group. To elucidate the mechanism of resistant inhibitory effect, the acorenone which had the strongest resistant inhibitory activity, was investigated on the CAT assay. As the result, the combination of Cm and acorenone showed the strongest inhibitory activity on CAT as noncompetitive and dose dependent manner.