PMID:9657392
| Citation |
Voges, D and Jap, BK (1998) Recombinant expression, purification and characterization of Kch, a putative Escherichia coli potassium channel protein. FEBS Lett. 429:104-8 |
|---|---|
| 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 alpha-helical content that is preserved upon addition of SDS. |
| Links | |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Escherichia coli/chemistry; Escherichia coli/genetics; Escherichia coli Proteins; Membrane Proteins/isolation & purification; Potassium Channels/chemistry; Potassium Channels/genetics; Potassium Channels/isolation & purification |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.