• Bulletin of the Korean Chemical Society
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• v.28 no.9
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• pp.1467-1471
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• 2007

The green-emitting CeMgAl11O19:Tb (CMAT) phosphor has been prepared at 1200 °C by the simple solid-state reaction using AlF3 as a self-flux. This preparation temperature is much lower than those (1500-1700 °C) for conventional solid-state reaction and spray pyrolysis method. In particular, the complete process to produce high-quality phosphor particles was carried out through the single-step heat treatment of the mixture of corresponding oxide-type metal sources. An addition of AlF3 as a self-flux significantly decreased the crystallization temperature of CMAT with plate-like shape. The particle morphology could be controlled from plate-like to spherical by using H3BO3 as an additional flux. Thus, an optimal morphology and luminescence characteristics of CMAT were achieved when both AlF3 and H3BO3 fluxes were simultaneously used. Compared with conventional solid-state process, which is accompanied by the calcination step(s), and other alternative liquid solution techniques such as sol-gel method and spray pyrolysis, no use of active precursors and liquid media that are harmful to the environment is a distinctive advantage for the industrial purpose.

• International Journal of Oral Biology
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• v.43 no.4
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• pp.201-207
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• 2018

Porphyromonas gingivalis is among the major etiological pathogens of chronic periodontitis. The virulence mechanisms of P. gingivalis is yet to be identified as its activity is largely unknown in actual disease process. The purpose of this study is to identify antigens of P. gingivalis expressed only in patients with chronic periodontitis using a unique immunoscreening technique. Change Mediated Antigen Technology (CMAT), an antibody-based screening technique, was used to identify virulence-associated proteins of P. gingivalis that are expressed only during infection stage in patients having chronic periodontitis. Out of 13,000 recombinant clones screened, 22 tested positive for reproducible reactivity with rabbit hyperimmune anti-sera prepared against dental plaque samples acquired from periodontitis patients. The DNA sequences of these 18 genes were determined. CMAT-identified protein antigens of P. gingivalis included proteins involved in energy metabolism and biosynthesis, heme and iron binding, drug resistance, specific enzyme activities, and unknown functions. Further analysis of these genes could result in a novel insight into the virulence mechanisms of P. gingivalis.

• Restorative Dentistry and Endodontics
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• v.40 no.4
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• pp.306-313
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• 2015

Objectives: Molecular mechanism of the pathogenicity of Enterococcus faecalis (E. faecalis), a suspected endodontic pathogen, has not yet been adequately elucidated due to limited information on its virulence factors. Here we report the identification of in vivo expressed antigens of E. faecalis by using a novel immunoscreening technique called change-mediated antigen technology (CMAT) and an experimental animal model of endodontic infection. Materials and Methods: Among 4,500 E. coli recombinant clones screened, 19 positive clones reacted reproducibly with hyperimmune sera obtained from rabbits immunized with E. faecalis cells isolated from an experimental endodontic infection. DNA sequences from 16 of these in vivo-induced (IVI) genes were determined. Results: Identified protein antigens of E. faecalis included enzymes involved in housekeeping functions, copper resistance protein, putative outer membrane proteins, and proteins of unknown function. Conclusions: In vivo expressed antigens of E. faecalis could be identified by using a novel immune-screening technique CMAT and an experimental animal model of endodontic infection. Detailed analysis of these IVI genes will lead to a better understanding of the molecular mechanisms involved in the endodontic infection of E. faecalis.