• 제목/요약/키워드: Two-Dimensional Electrophoresis

검색결과 319건 처리시간 0.029초

Proteomics 기술의 개발 및 응용 (Development and Applications of Proteomics Technology)

  • 이지원;이은규
    • KSBB Journal
    • /
    • 제16권2호
    • /
    • pp.99-106
    • /
    • 2001
  • Proteomics research includes identification and quantitation of single protein and/or protein complex, profiling of protein expression changes in response to biological perturbations, characterization of protein functions and interactions, and elucidation the linkage between proteins and diseases. In this review paper, recent developments in the basic technologies involved in the proteomics research such as 2-dimensional PAGE and mass spectrometry are discussed. Also, the application areas of proteomics technology such as protein expression mapping and cell map proteomics are introduced with the focus on new drug development.

  • PDF

작물 단백질체 분석을 위한 이차원 전기영동 사용법 (Crop proteomics: Practical method for high resolution of two-dimensional electrophoresis)

  • 김유지;정화진;이수지;김선태
    • Journal of Plant Biotechnology
    • /
    • 제39권1호
    • /
    • pp.81-92
    • /
    • 2012
  • 단백질체학에서 이차원 전기영동 (2-DGE)은 고해상도 단백질 분리가 가능한 중요 기술 중 하나이다. 본 논문에서는 2-DGE 이미지 분석 일치도를 향상시킴으로써 작물 단백질 검출과 정량분석이 가능하도록 하는 전반적인 주요 장비, 시약 등을 자세히 기술한 프로토콜을 제시하고 있다. 이 프로토콜은 식물의 발달, 생물학적, 비생물학적 스트레스 반응 등과 관련된 작물 단백질 바이오마커를 개발하기 위한 목적에서 2-DGE를 처음 시도하는 연구자들에게 유용할 것으로 기대한다.

Two- Dimensional Electrophoresis Analysis of Proteins; Bacillus subtilis LTD and Its Antifungal Activity Deficient Mutant

  • Lee, Young-Keun;Dinh, Le Thi;Jang, Yu-Sin;Chung, Hye-Young;Chang, Hwa-Hyoung
    • 환경생물
    • /
    • 제22권4호
    • /
    • pp.487-493
    • /
    • 2004
  • To investigate the antifungal activity related protein in pesticidal bacteria, a bacterial strain LTD was isolated from soil collected at Gimje in Jeonbuk province, Korea, and identified as Bacillus subtilis LTD based on a API50 CHB kit and 168 rDNA sequencing. It has an antifungal activity against 9 plant pathogenic fungi in a paper disc assay. The antifungal activity- deficient mutant, B. subtilis mLTD was induced at a 5 kGy dose of $^{60}Co$ gamma radiation. Using the two-dimensional electrophoresis and the matrix assisted laser desorption ionization time-of-flight mass spectrometry, the comparison analysis of proteins between the wild and mutant were performed. A major intracellular serine proteinase IspA (MW: 32.5 kDa), a NAD (P) H dehydrogenase (MW: 20.0 kDa), and a stage II sporulation protein AA, SpoIIAA (MW: 14.3kDa) were detected only in the B. subtilis LTD. These results suggested that the functions of these proteins found only in the B. subtilis LTD could. be closely related to the antifungal activity against plant pathogenic fungi.

Fungal Secretome for Biorefinery: Recent Advances in Proteomic Technology

  • Adav, Sunil S.;Sze, Siu Kwan
    • Mass Spectrometry Letters
    • /
    • 제4권1호
    • /
    • pp.1-9
    • /
    • 2013
  • Fungal biotechnology has been well established in food and healthcare sector, and now being explored for lignocellulosic biorefinery due to their great potential to produce a wide array of extracellular enzymes for nutrient recycling. Due to global warming, environmental pollution, green house gases emission and depleting fossil fuel, fungal enzymes for lignocellulosic biomass refinery become a major focus for utilizing renewal bioresources. Proteomic technologies tender better biological understanding and exposition of cellular mechanism of cell or microbes under particular physiological condition and are very useful in characterizing fungal secretome. Hence, in addition to traditional colorimetric enzyme assay, mass-spectrometry-based quantification methods for profiling lignocellulolytic enzymes have gained increasing popularity over the past five years. Majority of these methods include two dimensional gel electrophoresis coupled to mass spectrometry, differential stable isotope labeling and label free quantitation. Therefore, in this review, we reviewed more commonly used different proteomic techniques for profiling fungal secretome with a major focus on two dimensional gel electrophoresis, liquid chromatography-based quantitative mass spectrometry for global protein identification and quantification. We also discussed weaknesses and strengths of these methodologies for comprehensive identification and quantification of extracellular proteome.

한국산 멧누에 (Bombyx mandarina)에 있어서 난각유전자의 형질발현. I. 난각구조의 특이성과 Chorion 단백질 (Chorion Gene Expression in the Cellular Differentiation and Accumulation of Chorion Protein of Silkmoth, Bombyx mandarina I. Specific Structures of Egg-shell and Chorion Protein)

  • 노시갑
    • 한국응용곤충학회지
    • /
    • 제29권3호
    • /
    • pp.157-164
    • /
    • 1990
  • 한국산 멧누에(Bomdyx mandarina)chorion 유전자의 형질 발현기구를 규명하기 위한 연구의 일환으로 본 실험을 실시했다. 멧누에의 난각구조를 주사형 전자현마경에 의해 관찰한 결과 매우 특이적인 구조가 인정되었다. 즉 원추상의 불규칙 돌기에 의한 돌기구조층과 이 돌기 구조층을 덮고 있는 한 층의 얇은 덮개 구조층이 그것이다. 2차원 전기영동법에 의해 chorion 단백질을 분석한 결과, 난각을 구성하는 주요 단백질 성분은 등전점 4~6, 분자량 6~30 kd로 밝혀졌다. 특히 특이난각구조와 관련된 특이단백질 성분을 검출하였으며 이들의 대부분은 고cysteine 단백질인 것으로 추정했다. 이상의 연구결과에 의해 멧누에 난각의 특이 구조 형성에 따른 유전자발현기구 규명을 위한 기초자료가 얻어졌다.

  • PDF

The Effect of Protein Expression of Streptococcus pneumoniae by Blood

  • Bae, Song-Mee;Yeon, Sun-Mi;Kim, Tong-Soo;Lee, Kwang-Jun
    • BMB Reports
    • /
    • 제39권6호
    • /
    • pp.703-708
    • /
    • 2006
  • During infection, the common respiratory tract pathogen Streptococcus pneumoniae encounters several environmental conditions, such as upper respiratory tract, lung tissue, and blood stream, etc. In this study, we examined the effects of blood on S. pneumoniae protein expression using a combination of highly sensitive 2-dimensional electrophoresis (DE) and MALDI-TOF MS and/or LC/ESI-MS/MS. A comparison of expression profiles between the growth in THY medium and THY supplemented with blood allowed us to identify 7 spots, which increased or decreased two times or more compared with the control group: tyrosyl-tRNA synthetase, lactate oxidase, glutamyl-aminopeptidase, L-lactate dehydrogenase, cysteine synthase, ribose-phosphate pyrophosphokinase, and orotate phosphoribosyltransferase. This global approach can provide a better understanding of S. pneumoniae adaptation to its human host and a clue for its pathogenicity.