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Recombinant expression, purification and characterization of Kch, a putativeEscherichia colipotassium channel protein

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
429
Issue
1
Identifiers
DOI: 10.1016/s0014-5793(98)00509-2
Keywords
  • Membrane Protein
  • Channel Protein
  • Potassium Channel
  • Kch
Disciplines
  • Biology

Abstract

Abstract The Escherichia coli gene kch, similar in primary structure to eukaryotic voltage-gated potassium channels, was cloned and overexpressed in E. coli. The protein was solubilized from the plasma membrane with dodecylmaltopyranoside, lauryldimethylamine oxide or N-laurylsarcosine and was purified in milligram amounts by imidazole elution from a nickel-chelate column. The molecular mass of the purified protein in a number of detergents with 12 carbon atom chains suggests that rKch forms primarily tetramers of the 50 kDa monomers. CD spectroscopy of the purified protein indicates a significant α-helical content that is preserved upon addition of SDS.

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