• Proceedings of the Korean Society of Applied Pharmacology
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• 2001.11a
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• pp.94-94
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• 2001

Prostaglandin endoperoxide H synthase (PGHS) catalyzes the committed step in prostaglandins and thromboxane A$_2$-- oxygenation of arachidonic acid to the hydroperoxy endoperoxide PGG$_2$, followed by reduction PGG$_2$to the alcohol PGH$_2$. The two reactions by PGHS -- cyclooxygenase and peroxidase -- occur at distinct but structurally and functionally interconnected sites. The peroxidase reaction occurs at a heme-containing active site located near the protein surface. The cyclooxygenase reaction occurs in a hydrophobic channel in the core of the enzyme. Initially a peroxide reacts with the heme group, yielding Compound I and an alcohol derived from the oxidizing peroxide. Compound I next undergoes an intramolecular reduction by a single electron traveling from Tyr385 along the peptide chain to the proximal heme ligand, His388, and finally to the heme group. Following the binding of arachidonic acid, Tyr385 tyrosyl radical initiates the cyclooxygenase reaction by abstracting the 13-pro(5) hydrogen atom to give an arachidonyl radical, which sequentially reacts with two molecules of oxygen to yield PGG$_2$. In order to characterize PGHS peroxidase active site, we examined various lipid peroxides with purified recombinant ovine PGHS proteins and determined the rate constants. The results have shown that twenty-carbon unsaturated fatty acid hydroperoxides have similar efficiency in peroxidation by PGHS, irrespective of either the location of hydroperoxy group or the number of double bonds. It was also confirmed by the subsequent study with PGHS peroxidase active site mutants.

• Archives of Plastic Surgery
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• v.33 no.1
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• pp.46-52
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• 2006

High-density micromass culture was needed to take three dimensions culture with ASCs(adipose derived stromal cells) and chondrogenesis. However, the synthetic polymer has hydrophobic character and low affinity to cells and other biomolecules. Therefore, the surface modification without changes of physical and chemical properties is necessary for more suitable condition to cells and biomolecules. This study was performed to investigate the effect of surface modification of poly (lactic-co-glycolic acid)(PLGA) scaffold by plasma treatment (P(+)) on the adhesion, proliferation and chondrogenesis of ASCs, and not plasma treatment (P(-)). ASCs were isolated from human subcutaneous adipose tissue obtained by lipectomy and liposuction. At 1 hour 30 minutes and 3days after cell seeding onto the P(-) group and the P(+) group, total DNA amount of attached and proliferated ASCs markedly increased in the P(+) group (p < 0.05). The changes of the actin under confocal microscope were done for evaluation of cellular affinity, at 1 hour 30 minutes, the shape of the cells was spherical form in all group. At 3rd day, the shape of the cells was fiber network form and finely arranged in P(+) group rather than in P(-) group. RT-PCR analysis of cartilage-specific type II collagen and link protein were expressed in 1, 2 weeks of induction. Amount of Glycoaminoglycan (GAG) markedly increased in P(+) group(p < 0.05). In a week, extracellular matrix was not observed in the Alcian blue and Safranin O staining. However in 2 weeks, it was observed that sulfated proteoglycan increased in P(+) group rather than in P(-) group. In conclusion, we recognized that plasma treatment of PLGA scaffold could increase the hydrophilic property of cells, and provide suitable environment for high-density micromass culture to chondrogenesis

• Journal of Microbiology
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• v.45 no.2
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• pp.87-97
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• 2007

Medium-chain-length polyhydroxyalkanoates (MCL-PHAs), which have constituents with a typical chain length of $C_{6}-C_{14}$, are polyesters that are synthesized and accumulated in a wide variety of Gram-negative bacteria, mainly pseudomonads. These biopolyesters are promising materials for various applications because they have useful mechanical properties and are biodegradable and biocompatible. The versatile metabolic capacity of some Pseudomonas spp. enables them to synthesize MCL-PHAs that contain various functional substituents; these MCL-PHAs are of great interest because these functional groups can improve the physical properties of the polymers, allowing the creation of tailor-made products. Moreover, some functional substituents can be modified by chemical reactions to obtain more useful groups that can extend the potential applications of MCL-PHAs as environmentally friendly polymers and functional biomaterials for use in biomedical fields. Although MCL-PHAs are water-insoluble, hydrophobic polymers, they can be degraded by microorganisms that produce extracellular MCL-PHA depolymerase. MCL-PHA-degraders are relatively uncommon in natural environments and, to date, only a limited number of MCL-PHA depolymerases have been investigated at the molecular level. All known MCL-PHA depolymerases share a highly significant similarity in amino acid sequences, as well as several enzymatic characteristics. This paper reviews recent advances in our knowledge of MCL-PHAs, with particular emphasis on the findings by our research group.

• Textile Coloration and Finishing
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• v.20 no.2
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• pp.59-65
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• 2008

The tannin acid and the enzymes have been used in order to improve the ruggedness in laundry and the absorption of dyes and pigments in the textile industry for several years. The enzyme processing on the protein fiber minimizes the damage of the entire fiber and improves the dyeability by effectively modifying only the hydrophobic surface. This study tried out the structural observation by applying the Castanea crenata sieb. et. zucc. containing abundant tannin to the hair dyeing as the natural dyeing pigment along with Protease of Rhizopus sp. The dyeability was improved as compared to the dyeing using only the synthetic tanning and iron mordant. When the depth of pigment was higher in accordance with the surface observation, the enzyme dissolution had impact on dyeing and so the keratin layer on the hair surface. Accordingly, it was found that the appropriate depth was between 0.01 and 0.03%. It was estimated that 0.1% protease would treated within 30min. Consequently, it would cause the good reaction with the functional group of tannin pigment.

• Applied Chemistry for Engineering
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• v.5 no.5
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• pp.795-800
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• 1994

The detergencies of these new functional anionic surfactants, sodium monoglycerol ${\alpha}$-sulfonated alkanoates, were investigated and compared with those of two commercial surfactants, that is, sodium ${\alpha}$-sulfonated alkanoic acid methyl ester and sodium alkyl benzene sulfonate. According to the variation of the hydrophobic alkyl chain length, the order of detergency was shown to be $C_{16}$>$C_{18}$>$C_{14}$>$C_{12}$. From the comparision experiment for the detergency and the various fundamental properties of two other surfactants, it was found that sodium monoglycerol ${\alpha}$-sulfonated hexadecanonate has the most outstanding characteristics of detergency. Possibly this result shows light on its industrial application as a nonpolluting detergent.

• Applied Chemistry for Engineering
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• v.5 no.5
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• pp.801-807
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• 1994

Lactose substituted styrene monomer, N-(p-vinylbenzyl)-D-lactonamide(VLA) was prepared by coupling the lactose lactone with p-vinylbenzylamine. The carboxyl group of biotin was activated with N-hydroxysuccinimide in the presence of N, N'-dicyclohexylcarbodiimide. Subsquently, biotin substituted styrene monomer, N-(p-vinylbenzyl)-biotinamide(VBA) was prepared by amidation of the activated biotin with p-vinylbenzylamine. Poly(vinylbenzylactonamide-co-vinylbenzylbiotinamide), p(VLA-co-VBA) were synthesized through radical polymerization from the synthetic monomers(VLA-VBA) by using various mole ratio. The percentages of yield were 67~71%. The copolymers were found amphlphilic which had hydrophilic lactose, hydrophobic vinylbenzyl and biotin site within the structure. IR and $^{13}C-NMR$ analysis on the monomers and copolymer were carried out.

• Journal of Microbiology and Biotechnology
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• v.21 no.8
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• pp.822-829
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• 2011

Evidence shows that probiotic bacteria can undergo substantial structural and morphological changes in response to environmental stresses, including antibiotics. Therefore, this study investigated the effects of penicillin G (0.015, 0.03, and 0.06 mg/l) on the morphology and adhesion of Lactobacillus acidophilus ATCC 4356, including the colony morphotype, biofilm production, hydrophobicity, $H_2_O2$ formation, S-layer structure, and slpA gene expression. Whereas only smooth colonies grew in the presence of penicillin, rough and smooth colony types were observed in the control group. L. acidophilus ATCC 4356 was found to be hydrophobic under normal conditions, yet its hydrophobicity decreased in the presence of the antibiotic. No biofilm was produced by the bacterium, despite testing a variety of different culture conditions; however, treatment with penicillin G (0.015-0.06 mg/l) significantly decreased its production of $H_2_O_2$ formation and altered the S-layer protein structure and slpA gene expression. The S-protein expression decreased with 0.015 mg/l penicillin G, yet increased with 0.03 and 0.06 mg/l penicillin G. In addition, the slpA gene expression decreased in the presence of 0.015 mg/l of the antibiotic. In conclusion, penicillin G was able to alter the S-layer protein production, slpA gene expression, and certain physicochemical properties of Lactobacillus acidophilus ATCC 4356.

• Journal of Microbiology and Biotechnology
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• v.20 no.2
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• pp.294-300
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• 2010

The Iro protein is a member of the HiPIP family with the [$Fe_4S_4$] cluster for electron transfer. Many reports proposed that the conserved aromatic residues might be responsible for the stability of the iron-sulfur cluster in HiPIP. In this study, Tyr10 was found to be a critical residue for the stability of the [$Fe_4S_4$] cluster, according to site-directed mutagenesis results. Tyr10, Phe26, and Phe48 were essential for the stability of the [$Fe_4S_4$] cluster under acidic condition. Trp44 was not involved in the stability of the [$Fe_4S_4$] cluster. Molecular structure modeling for the mutant Tyr10 proteins revealed that the aromatic group of Tyr10 may form a hydrophobic barrier to protect the [$Fe_4S_4$] cluster from solvent.

• Journal of the Korean Chemical Society
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• v.26 no.5
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• pp.296-303
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• 1982

The solubilities of 1-phenyl-2-acetamido-3-butanone were measured in $H_2O$ at 20, 30 and 40$^{\circ}$C at pressure from 1 to 4500 kg/$cm^2$. Pressure going up to 4500 kg/$cm^2$, the solubility in $H_2O$decreases consistantly as that of diketopiperazine does. As diketopiperazine is a model compound of peptide bond and 1-phenyl-2-acetamido-3-butanone has only one peptide bond and a pretty large hydrophobic group, the solubility behavior is quite surprising. Volume change and heat capacity change data are reasonable.

• Journal of the Institute of Electronics Engineers of Korea SD
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• v.41 no.12
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• pp.1-6
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• 2004

In this study, heat and discharge treatments are arbitrary simulated for finding out the initiations and processes of surface degradation on the surface of polymer for using as a PCB substrate. Thermal-treatment changed the surface to the hydrophobic one with the increase of contact angle and surface potential decay, respectively. The XPS spectrum showed that the increased hydrophobicity in thermal treatment was originated from the continuous decrease of side-chains caused by secessions of oxygen groups and the increase of unsaturated double bond in carbon chains. Also, thermal-treatment caused the discoloration on the point of treated surface. These phenomena were attributed to the generation of ether group. In the chemical change by discharge treatment, a lot of side-chains occurred on the treated surface, and so the hydrophilicity increased as time elapsed.