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Hyang-Yim Seo,김경숙 한국생물공학회 2011 Biotechnology and Bioprocess Engineering Vol.16 No.2
Recombinant human H-ferritins produced from Saccharomyces cerevisiae were purified and their molecular properties were characterized. Electrophoresis of the recombinant H-ferritins showed revealed bands with mobilities similar to those of the H-ferritins produced by Escherichia coli. The pI of H-ferritins from yeast was more basic than that of H-ferritins produced by E. coli. When the cells were treated with tunicamycin, the pI of H-ferritins was driven to a sharp band with the pI range similar to that of those produced by E. coli, implying that the H-ferritins from yeast are glycosylated. The iron uptake of H-ferritins was rapid in the initial stage, with a slight reduction when compared to ferritins from E. coli. Recombinant ferritins are commonly used during synthesis of inorganic nanoparticles in their cores for chemical and industrial purposes. Transmission electron microscopy revealed that the reconstitution yield and size distribution of the core minerals were affected depending on the protein shells. The Hferritins with higher reconstitution yields (64.4%) showed slightly larger sizes (mean 6.52 nm) with narrower size distribution.
Ferritin 단백질 내 나노입자 합성 및 전자현미경 연구
서향임 ( Hyang Yim Seo ),김성원 ( Sung Won Kim ),박영석 ( Young Seog Park ),김경숙 ( Kyung Suk Kim ) 조선대학교 공학기술연구원 2008 공학기술논문지 Vol.1 No.2
One of the important issues in the synthesis of nanoparticles was to how to regulate the particle size. Ferritin, an iron storage protein, has received of global attention in candidates for obtaining uniform particle size. Here we report our studies on synthesis of several nanoparticle with Al(3+), UO2(2+), and Fe(2+) using ferritin and characteristic of core mineral using TEM (transmission electron microscopy) and EDXA (Energy dispersive X-ray analysis). The reaction factors such as ionic strength, reaction volumes and protein concentrations were changed reconstitution yields of ferritin and size distribution of particle. On the basis of above-mentioned results, ferribydrite minerals within ferritin core were successfully induced using up to 3000 iron atoms per protein molecule. The crystallinity of mineral was directly confirmed using FE-TEM (field emission-energy filtering-transmission electron microscopy) and it was controlled by protein concentrations and iron amounts.
Crystal Structure of Ferrihydrite Nanoparticles Synthesized in Ferritin
김성원,Hyang-Yim Seo,김경숙,Young-Boo Lee,박영석 대한화학회 2008 Bulletin of the Korean Chemical Society Vol.29 No.10
In this study, horse spleen apoferritins were induced to form biominerals using up to 3000 Fe atoms per protein molecule. The morphology and crystallinity of the nanometer-sized biominerals formed in the ferritins were then analyzed using field emission-energy filtering-transmission electron microscopy (FE-TEM). The ferritins were found to have reconstitution yields of 60-70% in the experiments. The mean core size of the ferritins varied somewhat with protein concentrations, indicating that crystal growth in ferritins could be controlled via protein concentrations. The core mineral size increased with the amount of Fe used. Lattice fringes of the core, associated with good crystallinity, were found in all samples. The lattice fringe images of a single domain ferrihydrite mineral appeared frequently in the (011) planes (d-spacing of 0.246 nm) under [100] zone axis in all samples of this study. In addition, the lattice image occasionally revealed fringes corresponding to the (100) planes (d = 0.254 nm) from the [001] zone axis, indicating the characteristic pattern of hexagonal crystal lattice. Diffraction patterns in the minerals identified as ferrihydrite were fitted well into the space group of P31c.