원문정보
Recombinant Human L-ferritin from Saccharomyces cerevisiae: Molecular Characterization and Synthesis of Iron Oxide Nanoparticles
초록
영어
1)In the synthesis of nanoparticles, much attention has been paid to regulating the particle size. There has been a possible evident that using the central cavity (core) of the protein ferritin has a greatly significant influence on it because the core can generate the nanometer-sized mineral particles of variable metal ions. In this report, recombinant human L-ferritins produced from Saccharomyces cerevisiae were purified and their molecular properties were characterized. The cDNA for human ferritin L chain was also expressed in another host such as Escherichia coli, and the properties of recombinant L-ferritins were compared. From isoelectric focusing experiment, the L-ferritin from the recombinant yeast showed no indication of N-glycosylation. Some post-translational modifications other than N-glycosylation were speculated in the L-ferritins from yeast. A difference was made in the L-ferritins in their iron uptake rates and the initial rate of the L-ferritin from yeast was slightly increased. The reconstitution yield and size distribution of the core minerals were analyzed in the L-ferritins by transmission electron microscopy. The L-ferritin from yeast with higher reconstitution yield (54.5%) showed slightly larger sizes (mean 6.92 nm) with narrower size distribution than the L-ferritin from E. coli. It is, in conclusion, speculated that L-ferritin from yeast is relatively superior to the other, in view of the size of nanoparticle and its relative homogeneity.
목차
1. 서론
2. 재료 및 방법
2.1. 재조합 대장균 및 재조합 효모의 배양
2.2. 재조합 L-ferritin의 정제
2.3. 전기영동
2.4. 등전점 (Isoelectric focusing)
2.5. Ferritin에 의한 철 흡수 실험
2.6. Ferritin 중공 내 철 산화물 합성 및 전자현미경(Transmission Electron Microscopy) 연구
3. 결과 및 고찰
3.1. 효모로부터 재조합 L-ferritin의 발현 및 활성도
3.2. L-ferritin의 등전점
3.3. 재조합 L-ferritin의 초기 철흡수율
3.4. L-ferritin의 재치환율 및 나노입자 크기
4. 결론
References