PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2010 | 57 | 1 |

Tytuł artykułu

One-step purification of vitronectin from human plasma by affinity chromatography on phage-displayed peptides

Autorzy

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
 A novel affinity purification method for rapid isolation of vitronectin (VN) from human plasma is described. Recently we have used phage display technology to obtain clones expressing peptides with high binding activity for VN. The isolated "strong VN binders" were covalently coupled to CNBr-activated Sepharose. Human plasma was applied to the column and bound VN was eluted using 0.5 M acetic acid, giving purity exceeding 90 %. The developed method is a convenient alternative to conventional antibody-antigen affinity chromatography techniques for purification of VN, as it offers low ligand cost, is rapid and ensures good protein recovery from human plasma.

Wydawca

-

Rocznik

Tom

57

Numer

1

Opis fizyczny

p.89-93,fig.,ref.

Twórcy

  • Medical University of Lodz, Lodz, Poland

Bibliografia

  • Campa MJ, Serlin SB, Patz EF Jr. (2002) Development of novel tumor imaging agents with phage-display combinatorial peptide libraries. Acad Radiol 9: 927-932.  
  • Clonis YD (2006) Affinity chromatography matures as bioinformatic and combinatorial tools develop. J Chromatogr A 1101: 1-24. 
  • Conlan MG, Tomasini BR, Schultz RL, Mosher DF (1988) Plasma vitronectin polymorphism in normal subjects and patients with disseminated intravascular coagulation. Blood 72: 185-190. 
  • Cwirla SE, Peters EA, Barret RW, Dower WJ (1990) Peptides on phage: A vast library of peptides for identifying ligands. Proc Natl Acad Sci USA 87: 6378-6382.  
  • Fassina G, Ruvo M, Palombo G, Verdoliva A, Marino M (2001) Novel ligands for the affinity-chromatographic purification of antibodies. J Biochem Biophys Methods 49: 481-490.  
  • Giordano RJ, Cardó-Vila M, Lahdenranta J, Pasqualini R, Arap W (2001) Biopanning and rapid analysis of selective interactive ligands. Nat Med 7: 1249-1253.  
  • Houghten RA, Pinilla C, Blondelle SE, Appel JR, Dooley CT, Cuervo JH (1991) Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery. Nature 354: 84-86.  
  • Hyde-DeRuyscher R, Paige LA, Christensen DJ, Hyde-DeRuyscher N, Lim A, Fredericks ZL, Kranz J, Gallant P, Zhang J, Rocklage SM, Fowlkes DM, Wendler PA, Hamilton PT (2000) Detection of small-molecule enzyme inhibitors with peptides isolated from phage-displayed combinatorial peptide libraries. Chem Biol 7: 17-25.  
  • Jungblut P, Klose J (1989) Dye ligand chromatography and two dimensional electrophoresis of complex protein extracts from mouse tissue. J Chromatogr 482: 125-132.  
  • Koivunen E, Arap W, Rajotte D, Lahdenranta J, Pasqualini R (1999) Identification of receptor ligands with phage display peptide libraries. J Nucl Med 40: 883-888.  
  • Kubota K, Katayama S, Matsuda M, Hayashi M (1988) Three types of vitronectin in human blood. Cell Struct Funct 13: 123-128.  
  • Kubota K, Hayashi M, Oishi N, Sakaki Y (1990) Polymorphism of the human vitronectin gene causes vitronectin blood type. Biochem Biophys Res Commun 167: 1355-1360.  
  • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.  
  • Lam KS, Salmon SE, Hersh EM, Hruby VJ, Kazmierski WM, Knapp RJ (1991) A new type of synthetic peptide library for identifying ligand-binding activity. Nature 354: 82-84.  
  • Liu R, Enstrom AM, Lam KS (2003) Combinatorial peptide library methods for immunobiology research. Exp Hematol 31: 11-30.  
  • Luo GX, Victor K, Chong K, McNeeley P, Ramirez D, Preclaro J, Linnik MD, Campbell MA (2001) Identification of a peptide that protects the human acetylcholine receptor against antigenic modulation. J Immunol Methods 251: 177-186.  
  • Noppe W, Vanhoorelbeke K, Galaev IY, Mattiasson B, Deckmyn H (2004) A probe for capture and Fe3+-induced conformational change of lactoferrin selected from phage displayed peptide libraries. J Dairy Sci 87: 3247-3255.  
  • Noppe W, Plieva FM, Galaev IY, Vanhoorelbeke K, Mattiasson B, Deckmyn H (2006) Immobilised peptide displaying phages as affinity ligand. Purification of lactoferrin from defatted milk. J Chromatogr A 1101: 79-85.  
  • Noppe W, Plieva FM, Vanhoorelbeke K, Deckmyn H, Tuncel M, Galaev IY, Mattiasson B (2007) Macroporous monolithic gels, cryogels, with immobilized phages from phage-display library as a new platform for fast development of affinity adsorbent capable of target capture from crude feeds. J Biotechnol 131: 293-299.  
  • Noppe W, Plieva F, Galaev IY, Pottel H, Deckmyn H, Mattiasson B (2009) Chromato-panning: an efficient new mode of identifying suitable ligands from phage display libraries. BMC Biotechnol 9: 21.  
  • Roque AC, Silva CS, Taipa MA (2007) Affinity-based methodologies and ligands for antibody purification: Advances and perspectives. J Chromatogr A 1160: 44-55.  
  • Shin DS, Kim DH, Chung WJ, Lee YS (2005) Combinatorial solid phase peptide synthesis and bioassays. J Biochem Mol Biol 38: 517-525.  
  • Smith GP (1985) Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228: 1315-1317.  
  • Smith GP, Petrenko VA (1997) Phage Display. Chem Rev 97: 391-410.  
  • Tollefsen DM, Weigel CJ, Kabeer MH (1990) The presence of methionine or threonine at position 381 in vitronectin is correlated with proteolytic cleavage at arginine 379. J Biol Chem 265: 9778-9781.  
  • Tozzi C, Anfossi L, Giraudi G (2003) Affinity chromatography techniques based on the immobilisation of peptides exhibiting specific binding activity. J Chromatogr B Analyt Technol Biomed Life Sci 797: 289-304.  
  • Utt M, Nilsson I, Ljungh A, Wadström T (2002) Identification of novel immunogenic proteins of Helicobacter pylori by proteome technology. J Immunol Methods 259: 1-10. 

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-e21fe66f-345f-4274-8a74-e61336a03f5d
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.