Separation of cobalt binding proteins by immobilized metal affinity chromatography

Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences
Eva Zatloukalová, Zdenka Kucerová

Abstract

Cobalt binding proteins from mouse liver, which were expressed in response to CoCl2 poisoning, were separated using gel permeation chromatography and then immobilised metal ion affinity chromatography (IMAC) with immobilized cobalt ions. Conditions used in IMAC-Co2+ were optimised. The fractions eluted with 60 mM imidazole were analysed by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Differences between the samples were also evaluated by a two-dimensional electrophoresis. Samples from the Co2+-treated mice provided higher number of electrophoretic spots than those from the untreated mice. Relative molecular masses of these proteins are appropriately 37,000; 32,000 and 26,000 and their isoelectric points (pI) are 6.5-7.5.

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Citations

Feb 19, 2014·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Yufeng SongZhenguo Shen
Oct 8, 2005·Expert Review of Proteomics·Xuesong SunQing-Yu He
Mar 1, 2008·Journal of Chromatography. a·Christian BassetClaude Vidaud
Feb 24, 2006·Applied Microbiology and Biotechnology·Matthias FranzrebOwen R T Thomas
Dec 15, 2010·Analytical and Bioanalytical Chemistry·Jun DongXinmiao Liang

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