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      효모에서 생산한 재조합 human L-ferritin의 생화학적 특성 및 나노입자의 철산화물 합성

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      https://www.riss.kr/link?id=A100422028

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      다국어 초록 (Multilingual Abstract)

      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 ...

      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.

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      목차 (Table of Contents)

      • Abstract
      • 1. 서론
      • 2. 재료 및 방법
      • 3. 결과 및 고찰
      • 4. 결론
      • Abstract
      • 1. 서론
      • 2. 재료 및 방법
      • 3. 결과 및 고찰
      • 4. 결론
      • References
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      참고문헌 (Reference)

      1 Burnette W. N, "Western blotting: electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A" 112 : 195-203, 1981

      2 Harrison, P. M, "The ferritins: molecular properties, iron storage function and cellular regulation" 1275 : 161-203, 1996

      3 Meldrum, F. C, "Synthesis of inorganic nanophase materials in supramolecular protein cages" 349 : 684-687, 1991

      4 Janney, D. E, "Structure of synthetic 2-line ferrihydrite by electron nanodiffraction" 85 : 118-1187, 2000

      5 Meldrum, F. C, "Reconstitution of manganese oxide cores in horse spleen and recombinant ferritins" 58 : 59-68, 1995

      6 Sung-Won Kim, "Reconstitution of Iron Cores in Horse Spleen and Yeast-derived Recombinant Human H- and L-chain Ferritins" 대한화학회 25 (25): 237-242, 2004

      7 Chang, S.-R, "Purification and characterization of recombinant tadpole H-chain ferritin in Escherichia coli" 28 : 238-242, 1995

      8 LEE, JUNG-LIM, "Purification and Glycosylation Pattern of Human L-Ferritin in Pichia pastoris" 한국미생물·생명공학회 14 (14): 68-73, 2004

      9 Santambrogio, P, "Production and characterization of recombinant heteropolymers of human ferritin H and L chains" 268 : 12744-12748, 1993

      10 Cozzi, A, "Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: In vivo role of ferritin ferroxidase activity" 18 : 25122-25129, 2000

      1 Burnette W. N, "Western blotting: electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A" 112 : 195-203, 1981

      2 Harrison, P. M, "The ferritins: molecular properties, iron storage function and cellular regulation" 1275 : 161-203, 1996

      3 Meldrum, F. C, "Synthesis of inorganic nanophase materials in supramolecular protein cages" 349 : 684-687, 1991

      4 Janney, D. E, "Structure of synthetic 2-line ferrihydrite by electron nanodiffraction" 85 : 118-1187, 2000

      5 Meldrum, F. C, "Reconstitution of manganese oxide cores in horse spleen and recombinant ferritins" 58 : 59-68, 1995

      6 Sung-Won Kim, "Reconstitution of Iron Cores in Horse Spleen and Yeast-derived Recombinant Human H- and L-chain Ferritins" 대한화학회 25 (25): 237-242, 2004

      7 Chang, S.-R, "Purification and characterization of recombinant tadpole H-chain ferritin in Escherichia coli" 28 : 238-242, 1995

      8 LEE, JUNG-LIM, "Purification and Glycosylation Pattern of Human L-Ferritin in Pichia pastoris" 한국미생물·생명공학회 14 (14): 68-73, 2004

      9 Santambrogio, P, "Production and characterization of recombinant heteropolymers of human ferritin H and L chains" 268 : 12744-12748, 1993

      10 Cozzi, A, "Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: In vivo role of ferritin ferroxidase activity" 18 : 25122-25129, 2000

      11 Chasteen, N. D, "Mineralization in ferritin: An efficient means of iron storage" 126 : 182-194, 1999

      12 Pead, S, "Metal ion binding to apo, halo, and reconstituted horse spleen ferritin" 59 : 15-27, 1995

      13 Kim, K.-S, "Iron cores of tadpole ferritin: native, reconstituted and recombinant H-chain ferritins" 298 : 107-111, 2000

      14 Wade, V. J, "Influence of site-directed modifications on the formation of iron cores in ferritin" 221 : 1443-1452, 1991

      15 Lee, J.-L, "Functional expression and production of human H-ferritin in Pichia pastoris" 25 : 1019-1023, 2003

      16 Fleming, J. T, "Ferritin: the role of aluminum in ferritin function" 12 : 413-418, 1991

      17 Arosio, P, "Ferritin: Iron homeostasis and oxidative damage" 33 : 457-463, 2002

      18 Harrison, P. M, "Ferritin. in Iron Transport and Storage" CRC press 82-101, 1990

      19 Joshi, J. G, "Ferritin-a general metal defoxicant" 21 : 105-110, 1989

      20 Seo, H.-Y, "Enhanced expression and functional characterization of the human ferritin H- and L-chain genes in Saccharomyces cerevisiae" 63 : 57-63, 2003

      21 Cragg, S. J, "Detection of a glycosylated subunit in human serum ferritin" 199 : 565-571, 1981

      22 Kyung-Suk Kim, "Crystal Structure of Ferrihydrite Nanoparticles Synthesized in Ferritin" 대한화학회 29 (29): 1969-1972, 2008

      23 Lee, J, "Cooperative activity of subunits of human ferritin heteropolymers in Escherichia coli" 34 : 365-370, 2001

      24 Mann, S, "Controlled synthesis of inorganic materials using supramolecular assemblies" 3 : 316-318, 1991

      25 Douglas, T, "Biomimetic synthesis of nanoscale particles in organized protein cages. in Biomimetic Materials Chemistry" VCH Publishers, Inc 91-115, 1996

      26 Cölfen H, "Bio-inspired mineralization using hydrophilic polymers" 271 : 1-77, 2007

      27 Hess, H. H, "A linear Lowry- Folin assay for both water-soluble and sodium dodecyl sulfatesolubilized proteins" 85 : 295-300, 1978

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      학술지 이력

      학술지 이력
      연월일 이력구분 이력상세 등재구분
      2022 평가예정 재인증평가 신청대상 (재인증)
      2019-01-01 평가 등재학술지 유지 (계속평가) KCI등재
      2016-01-01 평가 등재학술지 선정 (계속평가) KCI등재
      2015-12-01 평가 등재후보로 하락 (기타) KCI등재후보
      2011-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2009-08-28 학술지명변경 한글명 : 한국생물공학회지 -> KSBB Journal
      외국어명 : Korean Journal of Biotechnology and Bioengineering -> Korean Society for Biotechnology and Bioengineering Journal
      KCI등재
      2009-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2007-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2005-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2002-01-01 평가 등재학술지 선정 (등재후보2차) KCI등재
      1999-07-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
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      학술지 인용정보

      학술지 인용정보
      기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
      2016 0.37 0.37 0.38
      KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
      0.37 0.36 0.662 0.02
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