Comparison of different transition metal ions for immobilized metal affinity chromatography of selenoprotein P from human plasma

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Cu2+, Ni2+, Zn2+, Co2+ and Cd2+ were evaluated in metal ion affinity chromatography for enrichment of selenoprotein P, and immobilized Co2+ affinity chromatography was found to be the most selective chromatographic method. The chromatography was performed by fast protein liquid chromatography and the fractionation was followed by analysis of the collected fractions for selenium by inductively coupled plasma mass spectrometry. By the combination of immobilized Co2+ affinity chromatography and heparin affinity chromatography a simple method was developed yielding a 14,800-fold enrichment of selenoprotein P. The purity of the protein was determined by SDS-PAGE and by sequencing from polyvinylidene difluoride blots of SDS-PAGE gels.
Original languageEnglish
JournalJournal of Chromatography B: Biomedical Sciences and Applications
Volume735
Issue number1
Pages (from-to)85-91
Number of pages7
ISSN1387-2273
Publication statusPublished - 1999

    Research areas

  • Affinity Labels, Amino Acid Sequence, Cadmium, Chromatography, Affinity, Cobalt, Copper, Electrophoresis, Polyacrylamide Gel, Humans, Metals, Molecular Weight, Nickel, Proteins, Selenoprotein P, Selenoproteins, Sepharose, Zinc

ID: 44053799