• Bulletin of the Korean Chemical Society
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• v.33 no.3
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• pp.833-838
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• 2012

The thermal degradation products of polytrimethylene terephthalate (PTT) obtained by heating the sample in the temperature range of $250-360^{\circ}C$ under non-oxidative conditions was characterized using MALDI-TOF (matrix assisted laser desorption/ionization) mass spectrometry. The structures of the degradation products were determined and the relative compositions were estimated. The MALDI-TOF mass spectra of the thermally degraded PTT sample showed three main series of oligomer products with different end groups, which were carboxyl/carboxyl, carboxyl/allyl, and allyl/allyl. In contrast to the thermal degradation of polyethylene terephthalate (PET), the oligomers containing terephthalic anhydrides were not detected, whereas the formation of oligomers containing the unsaturated allyl ester group was confirmed by mass assignment. From these results, it was concluded that the thermal degradation of PTT proceeds exclusively through the ${\beta}$-CH hydrogen transfer mechanism, which is in accordance with the proposed reaction mechanism for the thermal degradation of polybutylene terephthalate (PBT).

• Analytical Science and Technology
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• v.8 no.4
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• pp.865-868
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• 1995

The method of matrix-assisted laser desorption ionization mass spectrometry has been used to solve some bioanalytical problems, which is difficult to analyse by general methods. For the selection of proper laser wavelength and matrices, eight matriees was used with laser wavelength of 226 and 355nm. The result shows that with wavelength of 355nm better results could be obtained with most of the matrices. The molecular weight of eytochrome C, which was seperated by gel electrophoresis and electro-blotted onto NC membrane is determined by MALDI. The accuracy is better than 0.1%, which is much higher than that of SDS-PAGE. Protein mixture extracted from crude peanut oil is directly determined by MALDI. The molecuiar weight of its three components are determined, and the result also demonstrated that these proteins are in free manner. As proteins arc in 2S bond, with the traditional method, SDS-PAGE, it is not able to decide whether protein exists in combination mode or in free manner. In the technique of two phase aquesous solution, which is used for separating biomaterials, water soluble polymers stained with dyes are used in this technique. By the use of MALDI the number or the dye molecules react with the polymer PEG molecule are determined, and that is difficult to determined by other methods.

• Journal of Applied Biological Chemistry
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• v.60 no.3
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• pp.271-277
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• 2017

Ethyl formate has been used for the control of insect pests by fumigation. However, there were not many reports to show its target site of fumigant toxicity on insect pests since its first use in the agricultural industry. In the present study, we showed the presumable target sites of ethyl formate fumigation in insect pests using Myzus persicae nymphs. After ethyl formate fumigation, the nymphs of this species were collected and the changes at the biochemical and molecular level were determined. The activity of cytochrome c oxidase (COX) was approximately two-fold higher after ethyl formate fumigation. In addition, the expression levels of acetylcholinesterase (AChE) decreased gradually with increasing ethyl formate concentration. These two findings suggested that COX and AChE might be the major target sites of ethyl formate fumigation. In addition to these results, the analysis of lipid content using MALDI-TOF MS/MS identified 9 phospholipids differently generated 2-fold higher in the ethyl formate-treated nymphs than that in the control nymphs, thereby leading to changes in cell membrane composition in M. persicae nymphs. Therefore, the ethyl formate fumigation caused lethal effects on M. persicae nymphs by changing COX activity, AChE gene expression, and phospholipid production.

• Journal of the Korean Wood Science and Technology
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• v.37 no.1
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• pp.56-64
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• 2009

The purpose of this study was to investigate and develop an eco-friendly wood adhesive based on vegetable oil (especially soybean oil), the renewable and sustainable natural resources, using ozonification technology for the chemical structure modification. The soybean oil (SBO) was reacted with $O_3$ at the rate of 7.13 g/h for different times, 15 minutes, 30 minutes, 60 minutes, and 120 minutes. The investigation of the modified chemical structure of the ozonized SBOs were conducted using FT-IR, $^1H$-NMR, MALDI-TOF MS, and GC/MS. As ozonification time increased, the peak of the unsaturated double bonds was disappeared and aldehyde or carboxyl peak appeared because ozonification broke the oil into small molecules. The plywoods were made at $110^{\circ}C$ with 30 seconds/mm hot-press time using the different ozonized SBO/pMDI adhesives and were tested for the dry, wet, cyclic boil test according to the Korea Industrial Standard F3101 Ordinary plywood. The bond strengths gradually increased with increasing ozonification time. The weight ratio 1:1 (ozonized SBO/pMDI), all strengths in 15, 30 and 60 minuets, exceeded constantly the dry, wet, cyclic boiling standard requirement. The range of ozonification time and weight ratio can fulfil1 the requirment of the wet test standard were 30~60 minutes and more than 0.5 pMDI. From the comprehensive view on the results of above experiments, it could be confirmed through experiments that ozonized SBO/pMDI has characteristics of effective reactivity and wet stability showed as an excellent candidate of wood adhesive applications.

• Bulletin of the Korean Chemical Society
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• v.33 no.9
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• pp.3076-3078
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• 2012

• 한국생물공학회:학술대회논문집
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• 2003.04a
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• pp.724-724
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• 2003

• Korean Journal of Microbiology
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• v.53 no.3
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• pp.163-169
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• 2017

Strains D4 and D5 were isolated from peach-rotten soil during the peach harvest season. The isolates were identified based on morphological and biochemical characterization, and identification was determined by 16S rRNA gene sequencing. Results showed that D4 has high similarity to Lactobacillus plantarum ATCC $14917^T$ and Lactobacillus pentosus ATCC $8041^T$ at 99.05% and 98.98%, respectively. D5 was also similar to Lactobacillus pentosus ATCC $8041^T$ and Lactobacillus plantarum ATCC $14917^T$ at 98.71% and 98.64%, respectively. In contrast, isolates showed differences in carbohydrate utilization in comparison to Lactobacillus plantarum ATCC $14917^T$ and Lactobacillus pentosus ATCC $8041^T$. In view of this we performed VITEK MS matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS) analysis, multiplex PCR fingerprinting, and random amplified polymorphic DNA (RAPD)-PCR to further confirm the identification of D4 and D5. The results of these analyses showed that both strains were most similar to Lactobacillus plantarum.

• Journal of Plant Biotechnology
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• v.29 no.3
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• pp.161-170
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• 2002

For the hairy root of Panax ginseng, we have got mass spectrums from MALDI/TOF/MS analysis and Tandem mass spectrums from ESI/Q-TOF/MS analysis. While mass spectrum provides the molecular weights of peptide fragments digested by protease such as trypsin, tandem mass spectrum produces amino acid sequence of digested peptides. Each amino acid sequences can be a query sequence in BLAST search to identify proteins. For the specimens of animals or plants of which genome sequences were known, we can easily identify expressed proteins from mass spectrums with high accuracy. However, for the other specimens such as ginseng, it is difficult to identify proteins with accuracy since all the protein sequences are not available yet. Here we compared the mass spectrums and the peptide amino acid sequences with ginseng expressed sequence tag (EST) DB. The matched EST sequence was used as a query in BLAST search for protein identification. They could offer the correct protein information by the sequence alignment with EST sequences. 90% of peptide sequences of ESI/Q-TOF/MS are matched with EST sequences. Comparing 68% matches of the same sequences with the nr database of NCBI, we got more matches by 22% from ginseng EST sequence search. In case of peptide mass fingerprinting from MALDI/TOF/MS, only about 19% (9 proteins of 47 spots) among peptide matches from nr DB were correlated with ginseng EST DB. From these results, we suggest that amino acid sequencing using tandem mass spectrum analysis may be necessary for protein identification in ginseng proteome analysis.

• Proceedings of the Zoological Society Korea Conference
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• 2000.10a
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• pp.168.3-169
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• 2000

No Abstract, See Full Text

• Reproductive and Developmental Biology
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• v.37 no.4
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• pp.247-253
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• 2013

Here, we present an approach of blood plasma proteome profiling and their comparisons between the young and the adult pigs as prerequisite for the identification of bio-markers related to the health conditions, growth performance and meat quality. To profile the proteome in porcine plasma, blood samples were collected from 19 young piglets and 20 adult male barrows and the plasma was retrieved. Then, protein profiling was initiated using one and two-dimensional electrophoresis. Proteins were spotted and then identified by MALDI-TOF-TOF and LC-MS-MS. In the results, more than thirty-six and twenty eight protein spots were selected in young piglets and adult pigs, respectively and twenty three proteins were identified. The proteome profile images were compared between those ones using Image Master Version 7.0. The image of expressed proteome showed that most of proteins from plasma of young piglet separated clearly and concentrated in 2DE display compared to ones from adult. Image analysis in detail was carried out to look for the specific proteins related to age progression. It demonstrated that the characteristics of proteome expression could be distinct to their age stages. Further investigations needed to proceed to understand the age dependent change of protein conformation and biological meaning of those differences in proteome expression between young and mature adult pigs.