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Czasopismo
2012 | 10 | 2 | 407-412
Tytuł artykułu

Using 2-D electrophoresis followed by nano HPLC in nuclear protein analysis of MCF-7 breast cancer cell line by MALDI-TOF/TOF

Treść / Zawartość
Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
The biomarker identification is an important tool in early cancer detection. The MCF-7 breast cancer cell line was chosen as a model system. The nuclear proteins were extracted utilizing a commercially manufactured kit and separated on two dimensional (2-D) sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS PAGE). The first dimension was performed on isoelectric focusing strips with pH range 4–7. Afterwards the proteins were tryptic digested and identification was performed by matrix assisted laser desorption technique with time of flight mass analyzer (MALDI-TOF/TOF). For unambiguous identification proteins with too low concentration or spots contains protein mixture the nano high performance liquid chromatography (HPLC) was used. The 2-D gel electrophoresis (2-DGE) seems to be a good tool to separate large amount of proteins using relatively simple procedure and its hyphenation with HPLC can create the perfect analytical solution for proteome identification. About 150 nuclei protein spots were visualized and the most abundant of them were identified. [...]
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Wydawca

Czasopismo
Rocznik
Tom
10
Numer
2
Strony
407-412
Opis fizyczny
Daty
wydano
2012-04-01
online
2012-01-29
Twórcy
  • Department of Medical Biophysics, Faculty of Medicine, University of Pavol Jozef Šafárik, 040 11, Košice, Slovakia
autor
  • Department of Medical Biophysics, Faculty of Medicine, University of Pavol Jozef Šafárik, 040 11, Košice, Slovakia, ivan.talian@upjs.sk
  • Department of Medical Biophysics, Faculty of Medicine, University of Pavol Jozef Šafárik, 040 11, Košice, Slovakia
autor
  • Department of Medical Biophysics, Faculty of Medicine, University of Pavol Jozef Šafárik, 040 11, Košice, Slovakia
Bibliografia
  • [1] X. Zhang, A. Fang, C.P. Riley, M. Wang, F.E. Regnier, Ch. Buck, Analytica Chimica Acta 664, 101 (2010) http://dx.doi.org/10.1016/j.aca.2010.02.001[Crossref]
  • [2] R. Pieper, C.L. Gatlin, A.J. Makusky, P.S. Russo, C.R. Schatz, S.S. Miller, Q. Su, A.M. McGrath, M.A. Estock, P.P. Parmar, M. Zhao, S. Huang, J. Zhou, F. Wang, R. Esquer-Blasco, N.L. Anderson, J. Taylor, S. Steiner, Proteomics 3, 1345 (2003) http://dx.doi.org/10.1002/pmic.200300449[Crossref]
  • [3] R.I. Somiari, A. Sullivan, S. Russell, S. Somiari, H. Hu, R. Jordan, A. George, R. Katenhusen, A. Buchowiecka, C. Arciero, H. Brzeski, J. Hooke, C. Shriver, Proteomics 3, 1863 (2003) http://dx.doi.org/10.1002/pmic.200300560[Crossref]
  • [4] C. Pionneau, L. Canelle, J. Bousquet, J. Hardouin, J. Bigeard, M. Caron, R. Joubert-Caron, Cancer Genomics Proteomics 2, 199 (2005)
  • [5] R.J. Simpson, L.M. Connoly, J.S. Eddes, J.J. Pereira, R.L. Moritz, G.E. Reid, Electrophoresis 21, 1707 (2000) http://dx.doi.org/10.1002/(SICI)1522-2683(20000501)21:9<1707::AID-ELPS1707>3.0.CO;2-Q[Crossref]
  • [6] F. Poirier, R. Joubert-Caron, V. Labas, M. Caron, Proteomics 3, 1028 (2003) http://dx.doi.org/10.1002/pmic.200300374[Crossref]
  • [7] P.J. Adam, R. Boyd, K.K. Tyson, G.C. Fletcher, A. Stamps, L. Hudson, H.R. Poyser, N. Redpath, M. Griffiths, G. Steers, A.L. Harris, S. Patel, J. Berry, J.A. Loader, R.R. Townsend, L. Daviet, P. Legrain, R. Parekh, J.A. Terrett, J. Biol. Chem. 278, 6482 (2003) http://dx.doi.org/10.1074/jbc.M210184200[Crossref]
  • [8] L. Malorni, G. Cacace, M. Cuccurullo, G. Pocsfalvi, A. Chambery, A. Farina, A. Di Maro, A. Parente, A. Malorni, Proteomics 6, 5973 (2006) http://dx.doi.org/10.1002/pmic.200600333[Crossref]
  • [9] Y. Ruan, W. Pei, M. Wan, Cell Biochem. Funct. 26, 787 (2008) http://dx.doi.org/10.1002/cbf.1507[Crossref]
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.-psjd-doi-10_2478_s11532-011-0156-x
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