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Separation of cobalt binding proteins by immobilized metal affinity chromatography

Authors
Journal
Journal of Chromatography B
1570-0232
Publisher
Elsevier
Publication Date
Volume
808
Issue
1
Identifiers
DOI: 10.1016/j.jchromb.2004.03.066
Keywords
  • Immobilization
  • Cobalt-Binding Proteins
Disciplines
  • Biology

Abstract

Abstract Cobalt binding proteins from mouse liver, which were expressed in response to CoCl 2 poisoning, were separated using gel permeation chromatography and then immobilised metal ion affinity chromatography (IMAC) with immobilized cobalt ions. Conditions used in IMAC-Co 2+ 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 Co 2+-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 (p I) are 6.5–7.5.

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