PMID: 8471822Jan 1, 1993Paper

Purification of outer membrane iron transport receptors from Escherichia coli by fast protein liquid chromatography: FepA and FecA

Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine
X H ZhouJ Adjimani

Abstract

Fast protein liquid chromatography (FPLC) with DEAE-Sepharose Fast Flow, PBE-94 and Q-Sepharose Fast Flow columns are applied to the purification of the ferric enterobactin protein receptor (FepA). The apparent single band of FepA on SDS-PAGE is isolated and purified into two proteins with very similar molecular weights. The two proteins are identified to be FepA and ferric citrate protein receptor (FecA) by N-terminus amino acid determination and a computer search with the Gene Bank file. The assay of binding activities of these proteins shows that both FepA and FecA bind ferric enterobactin, with the former having about double the activity of the latter. Competition studies shows that Fe-MECAM is competitively bound to both proteins and that ferric parabactin only slightly competes with [55Fe]ferric enterobactin. It is found that ferrichrome A has no effect on the binding of the receptor proteins with ferric enterobactin.

Citations

Aug 10, 2002·Journal of Bacteriology·Daniel C ScottPhillip E Klebba
Sep 18, 2007·Journal of Inorganic Biochemistry·Jennifer S Martinez, Alison Butler
Nov 27, 2018·Chemical Reviews·Alex ChaoCelia W Goulding

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