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수산물에 이산화염소(ClO₂) 처리에 따른 변이원성 및 Chlorate와 Chlorite ion의 결정
김정목 木浦大學校 工業技術硏究所 2000 工業技術硏究誌 Vol.10 No.-
The use of chlorine dioxide (CIO2) as a potential substitute for aqueous chlorine to improve the quality of seafood products has not been approved by regulatory agencies due to health concerns related to the production of chlorite (CIO2-) and chlorate (CIO3-) as well as possible mutagenic/ carcinogenic reaction products. Cubes of Atlantic salmon (Salmo salar) and red grouper (Epinephelus morio) were treated with 20 or 200 ppm aqueous chlorine or CIO2 solutions for 5 min, and extracts of the treated fish cubes and test solutions were checked for mutagenicity using the Ames Salmonella/microsome assay. No mutagenic activity was detected in the treated fish samples or test solutions with CIO2. Only the sample treated with 200 ppm chlorine showed weak mutagenic activity towards S. typhimurium TA 100. No chlorite residue was detected in sea scallops, maxi-mahi, or shrimp treated with CIO2 at 3.9 - 34.9 ppm. However, low levels of chlorate residues were detected in some of the treated samples. In most cases, the increase in chlorate in treated seafood was time- and dose-related.
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김정목,원형식,강사욱 한국자기공명학회 2013 Journal of the Korean Magnetic Resonance Society Vol.17 No.1
BldD, a developmental transcription factor from Streptomyces coelicolor, is a homodimeric, DNA-binding protein with 167 amino acids in each subunit. Each monomer consists of two structurally distinct domains, the N-terminal domain (BldD-NTD) responsible for DNA-binding and dimerization and the C-terminal domain (BldD-CTD). In contrast to the BldD-NTD, of which crystal structure has been solved, the BldD-CTD has been characterized neither in structure nor in function. Thus, in terms of structural genomics, structural study of the BldD-CTD has been conducted in solution, and in the present work, mainchain NMR assignments of the recombinant BldD-CTD (residues 80-167 of BldD) could be achieved by a series of heteronuclear multidimensional NMR experiments on a [13C/15N]-enriched protein sample. Finally, the secondary structure prediction by CSI and TALOS+ analysis using the assigned chemical shifts data identified a β-α-α-β-α-α-α topology of the domain. The results will provide the most fundamental data for more detailed approach to the atomic structure of the BldD-CTD, which would be essential for entire understanding of the molecular function of BldD.
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