• Bulletin of the Korean Chemical Society
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• v.28 no.9
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• pp.1499-1509
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• 2007

Proteomic analyses of synaptic vesicle fraction from rat brain have been performed for the better understanding of vesicle regulation and signal transmission. Two different approaches were applied to identify proteins in synaptic vesicle fraction. First, the isolated synaptic vesicle proteins were treated with trypsin, and the resulting peptides were analyzed using a high-pressure capillary reversed phase liquid chromatography/tandem mass spectrometry (cRPLC/MS/MS). Alternatively, proteins were separated by two-dimensional gel electrophoresis (2DE) and identified by matrix-assisted laser desorption ionization mass spectrometry (MALDI-TOF/MS). Total 18 and 52 proteins were identified from cRPLC/MS-MS and 2DE-MALDI-TOF-MS analysis, respectively. Among them only 2 proteins were identified by both methods. Of the proteins identified, 70% were soluble proteins and 30% were membrane proteins. They were categorized by their functions in vesicle trafficking and biogenesis, energy metabolism, signal transduction, transport and unknown functions. Among them, 27 proteins were not previously reported as synaptic proteins. The cellular functions of unknown proteins were estimated from the analysis of domain structure, expression profile and predicted interaction partners.

• Elastomers and Composites
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• v.40 no.3
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• pp.174-180
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• 2005

Sonochemical synthesis of fullerene oxides $[C_{70}O_n](n=1{\sim}2)$ by fullerene$[C_{70}]$ and metal hexacarbonyl complexes $M(CO)_6$(M=Cr, Mo, W) took place under air atmosphere. The reactivity of fullerene$[C_{70}]$ and several metal hexacarbonyl complexes $M(CO)_6$(M=Cr, Mo, W) under same ultrasonic condition increased in the order of $Mo(CO)_6$ > $W(CO)_6$ > $Cr(CO)_6$. The MALDI-TOF-MS, UV-visible spectra, and HPLC analysis confirmed that the products of sonochemical reaction were $[C_{70}O_n](n=1{\sim}2)$.

• Elastomers and Composites
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• v.39 no.2
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• pp.153-160
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• 2004

Fullerene oxides were synthesized by fullerene ($C_{70}$) and several amine N-oxides such as 3-picoline N-oxide, pyridine N-oxide hydrate, quinoline N-oxide, and isoquinoline N-oxide under ultrasonic condition at $25{\sim}43^{\circ}C$. The reactivity of fullerene ($C_{70}$) with various amine N-oxides undo, ultrasonic irradiation showed the same in all of the proceeding experiments; 3-picoline N-oxide : pyridine N-oxide hydrate : quinoline N-oxide : isoquinoline N-oxide. The MALDI-TOF MS, UV-vis spectrophotometer and HPLC analysis confirmed that the products of fullerene oxidation are [$C_{70}(O)n$] (n=1).

• Korean Journal of Poultry Science
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• v.32 no.1
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• pp.23-27
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• 2005

The aim of this study was to investigate differentially expressed proteins between normal chicken liver and chicken liver inffeted by Salmonella pullorum. 2-dimensional electrophoresis (2DE) and mass spectrometry (MS) were used to identify the proteins. More than 300 protein spots were detected on silver stained 2DE gels using pH 3$\~$10 gradients. The most outstanding protein spot was further analyzed by MALDI-TOF MS and protein database using the Mascot search engine. The protein was finally identified as APOAI (Apolipoprotein AI). Based on the known function of the APOAI, this gene acts protective action against the accumulation of platelet thrombin at the site of vascular damage for the pullorum disease. Therefore APOAI protein, identified in this study, can be a valuable biomarker in relation to the pullorum disease in chicken.

• Elastomers and Composites
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• v.40 no.1
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• pp.45-52
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• 2005

Synthesis or fullerene oxides[$C_{60}(O)_n$] ($n=1{\sim}4$ or n=1) by fullerene[$C_{60}$] and several oxidants such as 3-chloroperoxy benzoic acid, benzoyl peroxide, trichloroisocyanuric acid, and chromium(VI) oxide took place under microwave irradiation. The reactivity in solid state of fullerene[$C_{60}$] with various oxidants under same microwave rendition increased in order or 3- chloroperoxy benzoic acid > benzoyl peroxide > trichloroisocyanuric acid $\simeq$chromium(VI) oxide. The MALDI-TOF-MS, UV-visible spectra and HPLC analysis confirmed that the products of fullerene oxidation were [$C_{60}(O)_n$] ($n=1{\sim}4$ or n=1).

• Elastomers and Composites
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• v.39 no.4
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• pp.309-317
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• 2004

Synthesis of fullerene oxides [$C_{70}O_n$] ($n=1{\sim}3$ or n=1) in solid state by fullerene [$C_{70}$] and several oxidants such as 3-chloroperoxy benzoic acid, chromium(VI) oxide, benzoyl peroxide, and trichloroisocyanuric acid was taken place under microwave irradiation. The reactivity in solid state oi fullerene [$C_{70}$] with various oxidants under same microwave condition increased in the order of 3-chloroperoxy benzoic acid > chromium(VI) oxide > trichloroisocyanuric acid ${\simeq}benzoyl$ peroxide. The MALDI-TOF-MS, UV-visible spectra and HPLC analysis confirmed that the products of fullerene oxidation were [$C_{70}O_n$] ($n=1{\sim}3$ or n=1).

• Analytical Science and Technology
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• v.19 no.6
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• pp.529-534
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• 2006

The protein separation with molecular weight using SDS-PAGE(sodium dodecyl sulfate-polyacrylamide gel electrophoresis) is the one of the most conventional and simple techniques. In, this study, two dimensional SDS-PAGE using same separation principle consecutively was investigated and compared with one dimensional SDS-PAGE. The enhanced separation from duplex SDS-PAGE was observed and separated proteins in the gel were identified by MALDI TOF MS. Identified proteins from different gel spots were found to have different gi numbers. Therefore, duplex SDS-PAGE separation method will be used for economic separation method in the future because only tiny amount of inexpensive reagents are used to perform duplex SDS-PAGE.

• Journal of Veterinary Clinics
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• v.40 no.6
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• pp.393-398
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• 2023

We identified mastitis-causing pathogens using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) in an organic dairy farm and evaluated the effects of antimicrobial restriction on antimicrobial susceptibility. A total of 43 Holstein cows without any clinical sign of mastitis were used in this study, and 172 quarter milk samples were cultured on blood agar plates for 24 hours at 37℃. Subsequently, bacterial species were identified and antimicrobial susceptibility tests were performed. The subclinical mastitis infection rates in the cows and quarters were 58.1% (25/43) and 25.6% (44/172), respectively. In the species identification, Staphylococcus aureus (40.9%) was the most prominent isolate, followed by S. chromogenes (22.7%), S. epidermis (18.2%), S. simulans (11.4%), S. haemolyticus (2.3%), S. muscae (2.3%), and S. xylosus (2.3%). In the antimicrobial susceptibility test, all isolates were 100% susceptible to 24 of 28 antibiotics, except for benzylpenicillin, cefalotin, cefpodoxime, and trimethoprim/sulfamethoxazole. The resistance rates of S. aureus, S. chromogenes, and S. muscae isolates to trimethoprim/sulfamethoxazole were 27.8%, 10%, and 100%, respectively, and the resistance rates of S. epidermis and S. xylosus to benzylpenicillin were 50% and 100%, respectively. S. chromogenes, S. epidermis, S. simulans, S. haemolyticus, and S. xylosus were resistant to cefalotin and cefpodoxime. In conclusion, restrictions on antimicrobial use for organic dairy farm certification have resulted in a high Staphylococcus spp. infection rate. Therefore, our study indicates the importance of mastitis management strategies implemented by farmers together with veterinary practitioners, even if mastitis does not appear clinically in organic dairy farms.

• Korean Journal of Food Science and Technology
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• v.40 no.6
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• pp.712-716
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• 2008

In an effort to evaluate Salmonella food safety using combinations of preservation techniques, its viabilities when exposed to HCl, acetic acid, and the oxidative agents (hydrogen peroxide and butyl hydrogen peroxide), were analyzed using sub-lethal heat-shocked Salmonella Typhimurium at $56^{\circ}C$. 2D gel electrophoresis and MALDI-TOF MS analyses were also conducted to determine the expression and repression of proteins in heat-shocked cells. Heat-shocked S. Typhimurium evidenced a reduction of viable counts by 1-2 log CFU/mL. However, viality of non heat-shocked S. Typhimurium decreased markedly by 5-6 log CFU/mL at a pH 4 in response to acid and oxidative stresses. Sub-lethal heat treatment greatly increased the resistance of S. Typhimurium against acid and oxidant agents. As for 2D gel electrophoresis and protein identification via MALDI-TOF MS, 17 major proteins in non heat-shocked S. Typhimurium were detected, and only 13 proteins among these proteins were detected in heat-shocked S. Typhimurium. The heat shock proteins such as DnaK and small heat shock proteins were included, and may be associated with the resistance of S. typhimurium against exposure to acids and oxidants. Therefore, even though the promising hurdle technology using the combined mild treatments including heat was applied to S. Typhimurium, the proper heat treatment to reduce its crossprotection activity toward the following preservative agents might be considered.

• Journal of Life Science
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• v.18 no.6
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• pp.814-825
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• 2008

Ascochlorin (ASC) is prenyl-phenol compound that was isolated from the fungus Ascochyta viciae. ASC reduces serum cholesterol and triglyceride levels, and suppresses hypertension, tumor development, ameliorates type I and II diabetes. Here, to better understand the mechanisms by which ASC regulates physiological or pathological events and induces responses in the pharmacological treatment of inflammation, we performed differential analysis of the proteome of the mouse macrophage RAW264.7 cells in response to ASC. In this study, we used a proteomic analysis of LPS-induced RAW264.7 cells treated by ASC, to identify proteins potentially involved in inflammatory processes. The RAW264.7 cell proteomes with and without treatment with ASC were compared using two-dimensional electrophoresis (2-D SDS-PAGE), matrix-assisted laser desorption/ionization mass spectrometry (MALDI-TOF-MS) and bioinformatics. The largest differences in expression were observed for the calreticulin (4-fold decrease), ${\beta}-actin$ (4-fold decrease) and vimentin (1.5-fold decrease). In addition, rabaptin was increased 3-fold in RAW264.7 cells treated with ASC. The expression of some selected proteins was confirmed by RT-PCR analysis.