[논문]In Vitro Formation of Protein Nanoparticle Using Recombinant Human Ferritin H and L Chains Produced from E. coli

RO HYEON SU; PARK HYUN KYU; KIM MIN GON; CHUNG BONG HYUN

In Vitro Formation of Protein Nanoparticle Using Recombinant Human Ferritin H and L Chains Produced from E. coli 원문보기

Journal of microbiology and biotechnology, v.15 no.2, 2005년, pp.254 - 258

RO HYEON SU (BioNanotechnology Research Center, Korea Research Institute of Bioscience and Biotechnology) , PARK HYUN KYU (BioNanotechnology Research Center, Korea Research Institute of Bioscience and Biotechnology) , KIM MIN GON (BioNanotechnology Research Center, Korea Research Institute of Bioscience and Biotechnology) , CHUNG BONG HYUN (BioNanotechnology Research Center, Korea Research Institute of Bioscience and Biotechnology)

Abstract ▼ AI-Helper

We have conducted in vitro reconstitution study of ferritin from its subunits FerH and FerL. For the reconstitution, FerH was produced from an expression vector construct in Escherichia coli and was purified from a heat treated cell extract by using one-step column chromatography. FerL was expressed as inclusion bodies. The denatured form of FerL was obtained by a simple washing step of the inclusion bodies with 3 M urea. The reconstitution experiment was conducted with various molar ratios of urea-denatured FerH and FerL to make the ferritin nanoparticle with a controlled composition of FerH and FerL. SDS-PAGE analysis of the reconstituted ferritins revealed that the reconstitution required the presence of more than 40 molar$\%$ of FerH in the reconstitution mixture. The assembly of the subunits into the ferritin nanoparticle was confmned by the presence of spherical particles with diameter of 10 nm by the atomic force microscopic image. Further analysis of the particles by using a transmission electron microscope revealed that the reconstituted particles exhibited different percentages of population with dense iron core. The reconstituted ferritin nanoparticles made with molar ratios of [FerH]/[FerL]=l00/0 and 60/40 showed that 80 to $90\%$ of the particles were apoferritin, devoid of iron core. On the contrary, all the particles formed with [FerH]/[FerL]=85/ 15 were found to contain the iron core. This suggests that although FerH can uptake iron, a minor portion of FerL, not exceeding $40\%$ at most, is required to deposit iron inside the particle.

참고문헌 (19)

Feng, L. and S. Damodaran. 2000. Two dimensional array of magnetoferritin on quarts surface. Thin Solid Films 365: 99-103

상세보기
Grace, J. E., M. E. Van Eden, and S. D. Aust. 2000. Production of recombinant human apoferritin heteromers. Arch. Biochem. Biophys. 384: 116- 122

상세보기
Grady. J. K., Z. Zang, T. M. Laue, P. Arosio, and N. D. Chasteen. 2002. Characterization of the H- and L-subunit ratios of ferritins by sodium dodecyl sulfate-capillary gel electrophoresis. Anal. Biochem. 302: 263- 268

상세보기
Harrison, P. M. and P. Arosio. 1996. The ferritins: Molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1275: 161-203

상세보기
Hempstead, P. D., S. J. Yewdall, A. R. Fernie, D. M. Lawson, P. J. Artymiuk, D. W. Rice, G. C. Ford, and P. M. Harrison. 1997. Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution. J. Mol. Bol. 268: 424- 448

상세보기
Hudson, A. J., S. C. Andrews, C. Hawkins. J. M. Williams, M. Izuhara, F. C. Meldrum, S. Mann, P. M. Harrison. and J. R. Guest. 1993. Overproduction, purification and characterization of the Escherichia coli ferritin. Eur. J. Biochem. 218: 985- 995

상세보기
Kim, S. W., Y. H. Kim, and J. W. Lee. 2001. Thermal stability of human ferritin: Concentration dependence and enhanced stability of an N-terminal fusion mutant. Biochem. Biophys. Res. Commun. 289: 125-129

상세보기
Lee, J., H. Y. Seo, E. S. Jeon, O. S. Park, K. M. Lee, C. U. Park, and K. S. Kim. 2001. Cooperative activity of subunits of human ferritin heteropolymers in Escherichia coli. J. Biochem. Mol. Biol. 34: 365- 370

원문보기 상세보기
Levi, S., A. Luzzago, G. Cesareni, A. Cozzi, F. Franceschinelli, A. Albertini, and P. Arosio. 1988. Mechanism of ferritin iron uptake: Activity of the H-chain and deletion mapping of the ferro-oxidase site. J. Biol. Chem. 263: 18086- 18092
Levi, S., J. Salfeld, F. Franceschinelli, A. Cozzi, M. H. Dorner, and P. Arosio. 1989. Expression and structural and functional properties of human ferritin L-chain from Escherichia coli. Biochemistry 28: 5179- 5184

상세보기
Levi, S., S. J. Yewdall, P. M. Harrison, P. Santambrogio, A. Cozzi, E. Rovida, A. Albertini, and P Arosio, 1992. Evidence that H- and L-chains have co-operative roles in the iron-uptake mechanism of human ferritin. Biochem. J. 288: 591- 596

상세보기
Meldrum, F. C, B. R. Heywood, and S. Mann. 1992. Magnetoferritin: In vitro synthesis of a novel magnetic protein. Science 257: 522- 523

상세보기
Oh, B. K., Y. K. Kim, Y. M. Bae, W. H. Lee, and J. W. Choi. 2002. Detection of Escherichia coli O157:H7 using imrnunosensor based on surface plasmon resonance. J. Microbiol. Biotechnol. 12: 780- 786

원문보기 상세보기
Oh, K. S., Y. S. Park, and H. J. Sung. 2002. Expression and purification of an ACE-inhibitory peptide multimer from synthetic DNA in Escherichia coli. J. Microbiol. Biotechnol. 12: 59- 64
Rucker, P., F. M. Torti, and S. V. Torti. 1997. Recombinant ferritin: Modulation of subunit stoichiometry in bacterial expression systems. Protein Eng. 10: 967- 973

상세보기
Santambrogio, P., S. Levi, A. Cozzi, E. Rovida, A. Albertin, and P. Arosio. 1993. Production and characterization of recombinant heteropolymers of human ferritin H and L chains. J. Biol. Chem. 268: 12744- 12748

상세보기
Von Darl, M., P. M. Harrison, and W. Bottke. 1994. Expression in Escherichia coli of a secreted invertebrate ferritin. Eur. J. Biochem. 222: 367- 376

상세보기
Wong, K. K. W., T. Douglas, S. Gider, D. D. Awschalom, and S. Mann. 1998. Biomimetic synthesis and characterization of magnetic proteins magnetoferritin. Chem. Mater. 10: 279- 285

상세보기
Wong, K. K. W., H. Colfen, N. T. Whilton, T. Dougals, and S. Mann. 1999. Synthesis and characterization of hydrophobic ferritin proteins. J. Inorg, Biochem. 76: 187- 195

상세보기

저자의 다른 논문 :

표제어: PCR

동의어: Packet Collision Rate

용어 설명 출처 목록 (6)

용어 설명: PCR은 세균 특이성이 있는 primer를 이용하여 적은 수의 세균이 있을지라도 쉽게 검출할 수 있는 유용한 방법이며, 이를 이용하여 구강 내 치면세균막이나 타액에서 직접 세균을 검출할 수 있게 되었다[8].

AI-Helper ※ AI-Helper는 을 사용합니다.

AI-Helper

안녕하세요, AI-Helper입니다. 좌측 "선택된 텍스트"에서 텍스트를 선택하여 요약, 번역, 용어설명을 실행하세요.
※ AI-Helper는 부적절한 답변을 할 수 있습니다.

내보내기 구분	파일저장 인쇄 메일전송
구성항목	기본정보 상세정보 관리번호, 논문명, 저널/프로시딩명, 저자 , 발행년, 권, 호, 시작페이지, 끝페이지, 발행기관 관리번호, 논문명, 대등논문명, 저자 , 저널/프로시딩명, 발행기관, 발행년, 발행언어, 권, 호, 시작페이지, 끝페이지, ISBN, ISSN, 주제분야, 키워드, 초록(한글), 초록(영문), 저자(소속기관)
저장형식	Text(ASCII format) Excel format RefWorks Direct Export RIS format (for Reference Manager, ProCite, EndNote), Scholar's Aids, Mendeley
메일정보	받는사람 (필수) @ 보내는사람 (선택) @ 제목 내용 KISTI 검색결과 이메일 서비스
안내	총 건의 자료가 검색되었습니다. 다운받으실 자료의 인덱스를 입력하세요. (1-10,000) 검색결과의 순서대로 최대 10,000건 까지 다운로드가 가능합니다. 데이타가 많을 경우 속도가 느려질 수 있습니다.(최대 2~3분 소요) 다운로드 파일은 UTF-8 형태로 저장됩니다. 파일의 내용이 제대로 보이지 않을실 때는 웹브라우저 상단의 보기 -> 인코딩 -> 자동선택 여부를 확인하십시오. ~ Text(ASCII format) Excel format

연합인증