Proteomics 2005-02-01

Improvement of two-dimensional gel electrophoresis proteome maps of the haloarchaeon Haloferax volcanii.

Ivanka M Karadzic, Julie A Maupin-Furlow

Index: Proteomics 5 , 354-359, (2005)

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Abstract

Proteins of haloarchaea are remarkably unstable in low-ionic-strength solvents and tend to aggregate under standard two-dimensional (2-D) gel electrophoresis conditions, causing strong horizontal streaking. We have developed a new approach to generate 2-D maps of halophilic proteins which included washing cells with 1.5 M Tris-HCl buffer. In addition, proteins were precipitated with acetone, solubilized with urea and thiourea in the presence of the sulfobetaine detergent 3-[(3-cholamidopropyl)dimethylamino]-1-propanesulfonate (CHAPS), reduced with tributylphosphine (TBP), and separated with microrange strips of immobilized pH gradients (pH 3.9-5.1). This combination enabled the construction of highly reproducible 2-D maps of Haloferax volcanii proteins.

Related Compounds

  • Tributylphosphine
  • NDSB-211

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